wanglab/gogpt-training-data huggingface dataset:
Protein: Diacylglycerol lipase-beta (DAGL-beta) (DGL-beta) (EC 3.1.1.116) (KCCR13L) (PUFA-specific triacylglycerol lipase) (EC 3.1.1.3) (Sn1-specific diacylglycerol lipase beta) (Q8NCG7)
Organism: Homo sapiens (Human)
Function: Lipase that catalyzes the hydrolysis of arachidonic acid (AA)-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further cleaved by downstream enzymes to release arachidonic acid (AA) for cyclooxygenase (COX)-mediated eicosanoid production. Preferentially hydrolyzes DAGs at the sn-1 position in a calcium-dependent manner and has negligible activity against other lipids including monoacylglycerols and phospholipids. Plays a key role in the regulation of 2-AG and AA pools utilized by COX1/2 to generate lipid mediators of macrophage and microglia inflammatory responses. Functions also as a polyunsaturated fatty acids-specific triacylglycerol lipase in macrophages. Plays an important role to support the metabolic and signaling demands of macrophages (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:14610053}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Diacylglycerol lipase-alpha
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Fatty-acid amide hydrolase 1
- Monoglyceride lipase
- Monoacylglycerol lipase ABHD6
- Lysophosphatidylserine lipase ABHD12
- Cannabinoid receptor 1
Sequence:
MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA
Protein: POU domain, class 2, transcription factor 3 (Epoc-1) (Octamer-binding protein 11) (Oct-11) (Octamer-binding transcription factor 11) (OTF-11) (P31362)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Regulates cell type-specific differentiation pathways. Involved in the regulation of keratinocytes differentiation. The POU2F3-POU2AF2/POU2AF3 complex drives the expression of tuft-cell-specific genes, a rare chemosensory cells that coordinate immune and neural functions within mucosal epithelial tissues (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9242494}.
Interaction partners:
- POU domain, class 2, transcription factor 2
- Transient receptor potential cation channel subfamily M member 5
Sequence:
MVNLEPMHTEIKMSGDVADSTDTRSTFGQVEPGNDRNGLDFNRQIKTEDLGDSLQQTLSHRPCHLSQGPTMMPGNQMSGDMASLHPLQQLVLVPGHLQSVSQFLLSQTPPGQQGLQPNLLSFPQQQSTLLLPQTGPGLASQAVGRPGLSGSSLEPHLDAPQHLPGPKHLPGPGGNDEPTDLEELEKFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAESSPSDPSASTPSSYPTLSEVFGRKRKKRTSIETNIRLTLEKRFQDNPKPSSEEISMIAEQLSMEKEVVRVWFCNRRQKEKRINCPVATPVKPPIYNSRLVSPSGSLGPLSVPPVHSTMPGTVTSSCSPGNNSRPSSPGSGLHASSPTASQNNSKAAMNSSSSSSFNSSGSWYRWNHPTYLH
Protein: Zinc finger protein 11 (AtZFP11) (Q9SLB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may regulate cell division and growth.
Subcellular location: Nucleus {ECO:0000269|Ref.4}.
Interaction partners:
- Zinc finger protein 6
- Cleavage and polyadenylation specificity factor subunit 3-I
- Cleavage and polyadenylation specificity factor subunit 3-II
- Zinc finger protein 3
- C2H2 type zinc finger transcription factor family
Sequence:
MKRTHLASFSNRDKTQEEEGEDGNGDNRVIMNHYKNYEAGLIPWPPKNYTCSFCRREFRSAQALGGHMNVHRRDRAKLRQIPSWLFEPHHHTPIANPNPNFSSSSSSSTTTAHLEPSLTNQRSKTTPFPSARFDLLDSTTSYGGLMMDREKNKSNVCSREIKKSAIDACHSVRCEISRGDLMNKKDDQVMGLELGMSLRNPNQVLDLELRLGYL
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTC5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- Large ribosomal subunit protein uL30
- RP28
- Small ribosomal subunit protein eS25
- Candida glabrata strain CBS138 chromosome G complete sequence
- L33
- 40S ribosomal protein S7
- Small ribosomal subunit protein uS14
- 60S ribosomal protein L28
- Large ribosomal subunit protein eL24
Sequence:
MSGNGAQGTKFRISLGLPTGAIMNCADNSGARNLYIMAVKGSGSRLNRLPAASLGDMVMATVKKGKPELRKKVMPAIVVRQSKAWRRKDGVYLYFEDNAGVIANPKGEMKGSAITGPVGKECADLWPRVASNSGVVV
Protein: Sexual differentiation process protein isp4 (P40900)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable peptide transporter ptr2
- E3 ubiquitin-protein ligase ubr11
- Sexual differentiation process protein isp7
- Methylenetetrahydrofolate dehydrogenase [NAD
- Spore wall structural constituent isp3
Sequence:
MIGSINESPIEEHMNDSPSTKEKADSVDISDYIVSHSDDSLSKDIKKDTKSFLDVEHGEISTVDEFEEDSPYPEVRAAVPPTDDPSMPCNTIRMWTIGLIYSTVGAAVNMFFSLRNPTVTLSVLISELLAYPALQIWDLIFPDREFRIGRLKFNFKPGPFNVKEHALIVVMSSVSFGNAYSTDIILAQRVHYKQRFGFGYEICLTLATQLIGYGLAGLSRRLLVRPASMLWPVNLVQCTLIKTLHRKDLRNAVANGWRISPFRFFLYVFIASFIWNWFPSYIFQALSLFAWVTWIRPNSPTVNQIFGESTGISILPMTFDWNQISAYILSPLMAPADALMNILLGVILFFWIVTPALNFTNTWYGDYLPISSSGIIDHFGNSYNVTRILTKDATFDLDAYQNYSPIFMSTTYALAFGLSFASITSVIFHVILYHGKEIYDRLRDPPAPDIHEKLMKAYDEVPFYWYLSVFLAFFGMMMGTIYGWKTETPWWVIIVGVIFSAVWFIPIGIVQAITNIQLGLNVFTEFIVGYMYPGRPLAMMIFKTVGYITMTQGLAFAADLKFGHYMKLPPRIMFYTQMIATIWSCFVQIGVLDWALGNIDNVCQADQPDNYTCPNATVFFNSSVIWGVIGPKRMFSGKNTYTGLQYFWLAGVLGTILFWALWKKWPQKWWGQLNGPLIFGGTGYIPPATPVNYLAWSGIGLFFNYYLKKIFADWWQKYNFTLSAALDTGTQLSVIILFFCLQLPMVNFPDWWGNDGAFNTLDATGAAVRKLVNESAGEFFGPAEW
Protein: Probable beta-glucosidase A (EC 3.2.1.21) (Beta-D-glucoside glucohydrolase A) (Cellobiase A) (Gentiobiase A) (A2RAL4)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MRFTSIEAVALTAVSLASADELAYSPPYYPSPWANGQGDWAEAYQRAVDIVSQMTLAEKVNLTTGTGWELELCVGQTGGVPRLGIPGMCAQDSPLGVRDSDYNSAFPAGVNVAATWDKNLAYLRGQAMGQEFSDKGADIQLGPAAGPLGRSPDGGRNWEGFSPDPALSGVLFAETIKGIQDAGVVATAKHYIAYEQEHFRQAPEAQGYGFNITESGSANLDDKTMHELYLWPFADAIRAGAGAVMCSYNQINNSYGCQNSYTLNKLLKAELGFQGFVMSDWAAHHAGVSGALAGLDMSMPGDVDYDSGTSYWGTNLTISVLNGTVPQWRVDDMAVRIMAAYYKVGRDRLWTPPNFSSWTRDEYGFKYYYVSEGPYEKVNQFVNVQRNHSELIRRIGADSTVLLKNDGALPLTGKERLVALIGEDAGSNPYGANGCSDRGCDNGTLAMGWGSGTANFPYLVTPEQAISNEVLKNKNGVFTATDNWAIDQIEALAKTASVSLVFVNADSGEGYINVDGNLGDRRNLTLWRNGDNVIKAAASNCNNTIVIIHSVGPVLVNEWYDNPNVTAILWGGLPGQESGNSLADVLYGRVNPGAKSPFTWGKTREAYQDYLYTEPNNGNGAPQEDFVEGVFIDYRGFDKRNETPIYEFGYGLSYTTFNYSNLQVEVLSAPAYEPASGETEAAPTFGEVGNASDYLYPDGLQRITKFIYPWLNSTDLEASSGDASYGQDASDYLPEGATDGSAQPILPAGGGAGGNPRLYDELIRVSVTIKNTGKVAGDEVPQLYVSLGGPNEPKIVLRQFERITLQPSKETQWSTTLTRRDLANWNVETQDWEITSYPKMVFAGSSSRKLPLRASLPTVH
Protein: Cytochrome c mitochondrial import factor CYC2 (EC 1.-.-.-) (Cytochrome c assembly flavoprotein CYC2) (P38909)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Redox component that participates in c-type cytochrome biogenesis in the mitochondrial intermembrane space. May play a role in the reduction of heme prior to its ligation to apocytochrome c by cytochrome c heme lyase. Has oxidoreductase activity in vitro.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16207709, ECO:0000269|PubMed:8413243}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16207709, ECO:0000269|PubMed:8413243}; Intermembrane side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16207709, ECO:0000269|PubMed:8413243}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Holocytochrome-c synthase
- Cytochrome c isoform 2
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
Sequence:
MLWKNYVLSSSRITRRLHKSPRKSSFSKNFFITGCLLTVGAVSSYLTYRYTSERENKHELSPSYFVKYKISHKRDIDSSHFLLEVTPLFKQKVNIWSLMTAENLWSVEIKQPEVMVVRNYTPLPLKFNPASKEIEILKDGDNADGKLSFYIKKYENGEVARWLHHLPKGHIIEIRGPFIDYEFPHLPNELKRSRDCLYMDNRNERGNNVRENSQFIYQPYDIMMFTAGTGIVTALQLLLTESPFRGTIKLFHTDKNIKQLGPLYPILLRLQASNRVQLKIFETDRQTKQDVLKSIQKSITKPYPYKGLLPFSNVNNKNIMPVLALVCGPESYISSISGRKYDLNQGPVGGLLSKEGWNSDNVYKLS
Protein: Nematode cuticle collagen N-terminal domain-containing protein (O62432)
Organism: Caenorhabditis elegans
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
- Cuticle collagen dpy-13
- Spermatocyte protein spe-8
- COLlagen
- DumPY: shorter than wild-type
Sequence:
MDIDSKIKAYRFVGYAAVCFSAMAVLSVCITLPMVYNYVQHVRTQMHQELYACKGSAKDVWNSVYSIRELPLSANRTARSTYNEQCAGCCLPGPQGPQGTPGKPGKPGKPGAPGQPGTPGRPPQQPCEPTTPPPCQPCPQGPPGPPGQPGIPGDNGPPGEQGPKGPDAAPGEPGPKGPIGPPGPPGQAGAPGEPGSPAKSEPAVPGPPGPPGQAGQQGPPGPPGSNGIDGAPGAPGAKGEPGTPGEPGKDGEPGKPGTPGQDGTPGEKGICPKYCALDGGIFFEDGTRR
Protein: Smi1p (A0A1D8PE53)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Rlm1p
Sequence:
MGLLDNLKAFVHSITTEDHYASYDSPYRNDDNEPIGTNSHRSSTNDSALPLNNDLNNSQYSLDNSTGAAGFYRPGMKSSQQDLPLQNFSANGQPPLPSIDSLWDRIEYWIEQEYPELEDNLNDGVTTADLNEFMQDLQIGRNLPDDFRQFYKRHDGQLRGGKPTGLIMGLVLLDLEAIVEEKILWTKVAERLEGQYYMAQHKQRQDNIMKEGSSNNKSGPINNSFVANQRSIPPNSIQPYYYHKGWVILLKDNIGNQVAMDLLPGPAGQVGQIILFGRDFDTKLVIASSLQEFLFGFVTDLEQGNFQIDSSEYQEQLGFLSNDRNGDFMVGDEDEDQGELSFWDKDGQEFGKNVIRGRLSYIEVLKRRALKKYGLSETFETSFVPQRIPKKQQPQQKSSGSGSGSTTPIISQSRNASSSNLKKTTTNGNAASPATAAGSASTATTGAGNTKNKPPVPSPLANSDNASSSFSIPKETILNKNKPEKEEKEDKQEVSSSEKATVESKDPIETVNVSVNTDKEKPESKAESEAVKADDKESEEIKVTKNNDTEESEKKVEPEPESESEVVANAESLEEQQTVESSETTETSEVETKEESKKDTKEKSNDETKEVTDGLKEVEL
Protein: Small ribosomal subunit protein mS27 (28S ribosomal protein S27, mitochondrial) (MRP-S27) (S27mt) (Mitochondrial ribosomal protein S27) (Q8BK72)
Organism: Mus musculus (Mouse)
Function: RNA-binding component of the mitochondrial small ribosomal subunit (mt-SSU) that plays a role in mitochondrial protein synthesis. Stimulates mitochondrial mRNA translation of subunit components of the mitochondrial electron transport chain. Binds to the mitochondrial 12S rRNA (12S mt-rRNA) and tRNA(Glu). Overexpressed in hepatocellular carcinoma tissues compared with adjacent non-tumoral liver tissues.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q92552}. Mitochondrion {ECO:0000250|UniProtKB:Q92552}.
Interaction partners:
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS25
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein uS2m
Sequence:
MAAPMVRCGMLLARRLDASRLCLAGKRCLLSAAYVDSHQWEAREKEEYHLADLASLMDKAYERKLPVSSLSISRFVDNIASREDLDSAEYYLYKFRHSPNCWYLRDWTIHSWIRQCLKYGAQDKALYTLVNKVQYGIFPDNFTFNLLMDYFIKKGNYKDALSVVFEIMMQEAFDVPSTQFLSLYVLYRCLAEKTELTWEEERDFGASLLLSGLKQRNTVGLSSQLYGYALLGKVELQRGVRAVYHGMPLMWTPGYLDRALQVMERVASSPEDLKLGREVLDVLDGVLKVVTSPDVQTSEAQPQEGEDGLGSANLVEQLDTEEPEQSKLPRYLERFQASRSKLQELNRVESESLLTLTTQLVKEKLPACEAEDLATYEQKLREWHLERVQLIQREQEQREKAKQEYQALSAAEKAA
Protein: Ubiquitin ligase-binding protein BUL1 (Respiration deficiency suppressor 1) (P48524)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other permeases such as PMA1. The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription and pressure-induced differential regulation of the 2 tryptophan permeases TAT1 and TAT2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
- Nitrogen permease reactivator protein
- General amino-acid permease GAP1
- Arrestin-related trafficking adapter 3
- Arrestin-related trafficking adapter 6
- Protein ARG5,6
- Ubiquitin ligase-binding protein BUL2
- Protein ROD1
- Protein LST4
- Protein LDB19
Sequence:
MAKDLNDSGFPPKRKPLLRPQRSDFTANSSTTMNVNANTRGRGRQKQEGGKGSSRSPSLHSPKSWIRSASATGILGLRRPELAHSHSHAPSTGTPAGGNRSPLRRSTANATPVETGRSLTDGDINNVVDVLPSFEMYNTLHRHIPQGNVDPDRHDFPPSYQEANNSTATGAAGSSADLSHQSLSTDALGATRSSSTSNLENLIPLRTEHHSIAAHQSTAVDEDSLDIPPILDDLNDTDNIFIDKLYTLPKMSTPIEITIKTTKHAPIPHVKPEEESILKEYTSGDLIHGFITIENKSQANLKFEMFYVTLESYISIIDKVKSKRTIKRFLRMVDLSASWSYSKIALGSGVDFIPADVDYDGSVFGLNNSRVLEPGVKYKKFFIFKLPLQLLDVTCKQEHFSHCLLPPSFGIDKYRNNCKYSGIKVNRVLGCGHLGTKGSPILTNDMSDDNLSINYTIDARIVGKDQKASKLYIMKEREYNLRVIPFGFDANVVGERTTMSQLNDITKLVQERLDALRKIFQRLEKKEPITNRDIHGADLSGTIDDSIESDSQEILQRKLDQLHIKNRNNYLVNYNDLKLGHDLDNGRSGNSGHNTDTSRAWGPFVESELKYKLKNKSNSSSFLNFSHFLNSSSSSMSSSSNAGKNNHDLTGNKERTGLILVKAKIPKQGLPYWAPSLLRKTNVFESKSKHDQENWVRLSELIPEDVKKPLEKLDLQLTCIESDNSLPHDPPEIQSITTELICITAKSDNSIPIKLNSELLMNKEKLTSIKALYDDFHSKICEYETKFNKNFLELNELYNMNRGDRRPKELKFTDFITSQLFNDIESICNLKVSVHNLSNIFKKQVSTLKQHSKHALSEDSISHTGNGSSSSPSSASLTPVTSSSKSSLFLPSGSSSTSLKFTDQIVHKWVRIAPLQYKRDINVNLEFNKDIKETLIPSFESCLCCRFYCVRVMIKFENHLGVAKIDIPISVRQVTK
Protein: Lipid droplet assembly factor 1, isoform C (M9PIQ9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Seipin
Sequence:
MVGTGVSEVGVPASSEESVDFGWNRHRKSKAHSNKARKAAKEANAKKSAGSGTESKPEHVKIHGPGDRSAGVLTGDQFLESLLQTLYRSWLQICRLADFVMSELGGNDFLEATAAWCTRNPHVAICLLAGGLVFMLPFLIIFGFGIATMVMTFTGLLVLEGTLLTIVSMVFFACLGGLVIMVPLFGVAAVAAYFGFAQVYGLCDGIEIHKSAWVMFFRDQRKAGDPPPAAVTITDEPTSTTA
Protein: Beta-ureidopropionase (EC 3.5.1.6) (Beta-alanine synthase) (N-carbamoyl-beta-alanine amidohydrolase) (Q8VC97)
Organism: Mus musculus (Mouse)
Function: Catalyzes a late step in pyrimidine degradation. Converts N-carbamoyl-beta-alanine (3-ureidopropanoate) into beta-alanine, ammonia and carbon dioxide. Likewise, converts N-carbamoyl-beta-aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate, ammonia and carbon dioxide.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Dihydropyrimidinase
- Dihydropyrimidine dehydrogenase [NADP
- 4-aminobutyrate aminotransferase, mitochondrial
- Alpha-aminoadipic semialdehyde dehydrogenase
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase X, mitochondrial
- Acidic amino acid decarboxylase GADL1
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- Aldehyde dehydrogenase family 3 member B3
Sequence:
MAGPEWQSLEQCLEKHLPPDDLAQVKRILYGKQTRNLDLPREALKAASERNFELKGYAFGAAKEQQRCPQIVRVGLVQNRIPLPTSAPVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLPWTEFAESAEDGLTTRFCQKLAKKHNMVVVSPILERDREHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGQEHFPNEFTSGDGKKAHHDLGYFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMYARELAEAVKPNYSPNIVKEDLVLAPSSG
Protein: F-box only protein 31 (Q3TQF0)
Organism: Mus musculus (Mouse)
Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest (By similarity).
Interaction partners:
- S-phase kinase-associated protein 1
- G1/S-specific cyclin-D1
- Cullin-1
Sequence:
MAVCARLCGVGPARGCRRRQQRRGPAETAAADSEADTDPEEERIEAGPARCSLLELPPELLVEIFASLPGTDLPSLAQVCSRFRRILHTDTIWRRRCREEYGVCENLRKLEITGVSCRDVYAKLLHRYRHILGLWQPDIGPYGGLLNVVVDGLFIIGWMYLPPHDPHVGDPMRFKPLFRIHLMERKSATVECMYGHKGPHNGHIQIVKRDEFSTKCNQTDHHRMSGGRQEEFRTWLREEWGRTLEDIFHEHMQELILMKFIYTSQYDNCLTYRRIYLPPSHPDDLIKPGLFKGTYGSHGLEIVMLSFHGSRARGTKITGDPNIPAGQQTVEIDLQRRIQLPDVENLRNFNELSRIVLEVREQVRQEQEAGEGAAPPREPSAKAADGPPAKDGKEPGGGAEAAEQSASSGQGQPFVLPVGVSSRNEDYPRTCRLCFYGTGLIAGHGFTSPERTPGVFVLFDEDRFGFLWLELKSFSLYSRVQATFQNAAAPSPQAFDEMLRNIQSLTS
Protein: Secreted frizzled-related protein 2 (B1WBV2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Protein Wnt
- Protein Wnt
- Protein Wnt-5a
- Protein Wnt
- Protein Wnt-4
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Dickkopf homolog 1
Sequence:
MLRGPASLLLLVLASHCCLGSARGLFLFGQPDFSYKRSNCKPIPANLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCVQVKDRCAPVMSAFGFPWPDMLECDRFPQDNDLCIPLASSDHLLPPTEEAPKVCEACKTKNEDDNDIMETLCKNDFALKIKVKEITYINRDTKIILETKSKTIYKLNGVSDRDLKKSVLWLKDSLQCTCEEMNDINAPYLVMGQKQGGELVITSVKRWQKGQREFKRISRSIRKLQC
Protein: Neuroendocrine convertase 2 (NEC 2) (EC 3.4.21.94) (DMH #5) (Prohormone convertase 2) (dPC2) (Protein amontillado) (Q9VBC7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine endopeptidase which is involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Required during embryonic and larval development, probably by proteolytically processing peptide hormones involved in hatching, larval growth and larval molting. Required for the processing and activation of Akh which maintains normal hemolymph sugar levels. Has been shown in one study to be required for processing of sli into slit N-product and slit C-product in the embryo which is necessary for lateral transverse muscle elongation but has been shown in another study not to be required for sli cleavage. Required for larval hatching. Also required for normal larval wandering behavior which occurs prior to pupariation. Required during pupal development for head eversion, leg and wing disk extension, and abdominal differentiation. Required during eye development for R8 photoreceptor cell specification by regulating processing of ligands required for the BMP and activin signaling pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:10749852}.
Interaction partners:
- Neuroendocrine protein 7B2
- IA-2 protein tyrosine phosphatase, isoform C
Sequence:
MAAATWSWLLAPFLLLHWASAGAGGGAGGSGAGLSGPAVFTSSFLVRFRRGVDNSFAHDVADKYGFDNLGPLVGADGHEYHFKHRTLPHARSRRSLTHTRALKSHPAVHTAVQQPGFKRVKRGLRPAVPAIHGMKFDLKVGEGNRIDEEPTDPYFPMQWYLKNTGQNGGKVRLDLNVQAAWAQGITGKNVTTAIMDDGVDYMHPDLKFNYNAEASYDFSSNDPFPYPRYTDDWFNSHGTRCAGEVAAARDNGICGVGVAYDSKIAGIRMLDQPYMTDLIEANSMGHEPHKIHIYSASWGPTDDGKTVDGPRNATMRAIVQGVNEGRNGLGNIYVWASGDGGEEDDCNCDGYAASMWTISINSAINDGQNAHYDESCSSTLASTFSNGAKDPNTGVATTDLYGKCTTTHSGTSAAAPEAAGVFALALEANPQLTWRDIQHLTVLTSKRNSLFDAKNRFHWTMNGVGLEFNHLFGFGVLDAGAMVTLSKQWHSVPPRYHCEAGELTQPQAIVMGRSLFWEIKTDACKGTDTEVNYLEHVQAVISANASRRGDLELFLTSPMGTKSMILSRRANDDDHRDGFTKWPFMTTHSWGEYPQGTWKLEARFNSPQTRHGNLLEWSLVLHGTKEAPYRTLHPSSPHSKLAIVKKAHEDKKMK
Protein: Large ribosomal subunit protein eL39 (60S ribosomal protein L39) (Ribosomal protein 46) (O16130)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL36
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS25
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL28
Sequence:
MAAHKSFRIKQKLAKKLKQNRSVPQWVRLRTGNTIRYNAKRRHWRRTKLKL
Protein: Large ribosomal subunit protein mL51 (39S ribosomal protein L51, mitochondrial) (A0A0B4J2C1)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MFGVYDNIGILGNFEKHPKELIRGPIWLRGWKGNELQRCIRKRKMVGSRMFADDLHNLNKRIRYLYKHFNRHGKFR
Protein: Nucleolar protein 10 (D3ZMP6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 1
- Ribonucloprotein
- Ribonucloprotein
- H/ACA ribonucleoprotein complex subunit DKC1
- Telomerase Cajal body protein 1
- Telomerase reverse transcriptase
- NHP2-like protein 1
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Nucleolar protein 58
Sequence:
MFLQYYLNEQGDRVYTLKKFDPMGQQTCSAHPARFSPDDKYSRHRITIKKRFKVLMTQQPRPVL
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (A0A8I6ANK9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MALFSVRKARECWRFIRALHKGPTATAAPQKESGERVFSGIQPTGIPHLGNYLGAIESWVKLQEEYDTVIYSIVDLHSITVPQDPGILQQSILDMTAVLLACGIDPERSILFQQSQAKAARQKHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGELFPLPRSILTSMKKVKSLRDPSAKMSKSDPDKLATVQITDSPEEIVRKFRKAVTDFTSEVTYEPDSRPGVSNMVAIHAAVSGLSVEEVVRNSAGVDTARYKLLVADAVIEKFAPIRSEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGIL
Protein: Potassium-transporting ATPase alpha chain 1 (EC 7.2.2.19) (Gastric H(+)/K(+) ATPase subunit alpha) (Proton pump) (P19156)
Organism: Sus scrofa (Pig)
Function: The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell (By similarity). Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P20648}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21224846}; Multi-pass membrane protein. Note=Localized in the apical canalicular membrane of parietal cells. {ECO:0000250|UniProtKB:P20648}.
Interaction partners:
- Potassium-transporting ATPase subunit beta
- inorganic diphosphatase
- inorganic diphosphatase
- Sodium/potassium-transporting ATPase subunit alpha
- Gastrin
- Sodium/potassium-transporting ATPase subunit beta-1
Sequence:
MGKAENYELYQVELGPGPSGDMAAKMSKKKAGRGGGKRKEKLENMKKEMEINDHQLSVAELEQKYQTSATKGLSASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLALALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILQAQGRKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTAQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFIVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHSADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRERFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHVLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLSEKDYPPGYAFDVEAMNFPTSGLSFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRPQWENHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEMCQIADVLIRKTRRLSAFQQGFFRNRILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPMPFGLLIFVYDEIRKLGVRCCPGSWWDQELYY