wanglab/gogpt-training-data huggingface dataset:
Protein: Glucose 1-dehydrogenase (GDH) (GlcDH) (EC 1.1.1.47) (Q977U7)
Organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Function: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-xylose, D-galactose, and D-fucose, to the corresponding glyconate. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a preference for NADP(+). Physiologically, seems to be involved in the degradation of glucose through a modified Entner-Doudoroff pathway.
Interaction partners:
- Glucokinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Probable glucose-6-phosphate isomerase
- Enolase
- Triosephosphate isomerase
- Transcriptional regulator GfcR
- 2-oxo acid dehydrogenase
- 2-oxo acid dehydrogenase E1 component subunit alpha)
- 2-oxoisovalerate dehydrogenase
- 2-oxoacid ferredoxin oxidoreductase
Sequence:
MKAIAVKRGEDRPVVIEKPRPEPESGEALVRTLRVGVDGTDHEVIAGGHGGFPEGEDHLVLGHEAVGVVVDPNDTELEEGDIVVPTVRRPPASGTNEYFERDQPDMAPDGMYFERGIVGAHGYMSEFFTSPEKYLVRIPRSQAELGFLIEPISITEKALEHAYASRSAFDWDPSSAFVLGNGSLGLLTLAMLKVDDKGYENLYCLGRRDRPDPTIDIIEELDATYVDSRQTPVEDVPDVYEQMDFIYEATGFPKHAIQSVQALAPNGVGALLGVPSDWAFEVDAGAFHREMVLHNKALVGSVNSHVEHFEAATVTFTKLPKWFLEDLVTGVHPLSEFEAAFDDDDTTIKTAIEFSTV
Protein: Aquaporin TIP2-3 (Tonoplast intrinsic protein 2-3) (ZmTIP2-3) (ZmTIP2;3) (Q84RL6)
Organism: Zea mays (Maize)
Function: Water channel required to facilitate the transport of water across cell membrane.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Aquaporin SIP2-1
- Aquaporin SIP1-1
- Aquaporin SIP1-2
Sequence:
MVKLAFGSFRDSLSAASLKAYVAEFIATLLFVFAGVGSAIAYSQLTKGGALDPAGLVAIAIAHAFALFVGVSMAANISGGHLNPAVTFGLAVGGHITILTGILYWVAQLLGASVACFLLQYVTHGQAIPTHGVSGISEIEGVVMEIVITFALVYTVYATAADPKKGSLGTIAPMAIGFIVGANILAAGPFSGGSMNPARSFGPAVAAGNFAGNWVYWVGPLVGGGLAGLVYGDVFIASYQPVGQQEYP
Protein: Small ribosomal subunit protein uS19 (40S ribosomal protein S15) (RIG protein) (P62845)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62841}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS7
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS3
Sequence:
MAEVEQKKKRTFRKFTYRGVDLDQLLDMSYEQLMQLYSARQRRRLNRGLRRKQHSLLKRLRKAKKEAPPMEKPEVVKTHLRDMIILPEMVGSMVGVYNGKTFNQVEIKPEMIGHYLGEFSITYKPVKHGRPGIGATHSSRFIPLK
Protein: Phosphoinositide 3-kinase regulatory subunit 6 (Phosphoinositide 3-kinase gamma adapter protein of 87 kDa) (p84 PI3K adapter protein) (p84 PIKAP) (p87 PI3K adapter protein) (p87PIKAP) (Q5UE93)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the PI3K gamma complex. Acts as an adapter to drive activation of PIK3CG by beta-gamma G protein dimers. The PIK3CG:PIK3R6 heterodimer is much less sensitive to beta-gamma G protein dimers than PIK3CG:PIK3R5 and its membrane recruitment and beta-gamma G protein dimer-dependent activation requires HRAS bound to PIK3CG. Recruits of the PI3K gamma complex to a PDE3B:RAPGEF3 signaling complex involved in angiogenesis; signaling seems to involve RRAS.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3U6Q4}. Cell membrane {ECO:0000250|UniProtKB:Q3U6Q4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q3U6Q4}. Note=Translocated to the plasma membrane in a Ras-dependent manner. {ECO:0000250|UniProtKB:Q3U6Q4}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphoinositide 3-kinase regulatory subunit 5
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Tyrosine-protein kinase HCK
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Tyrosine-protein kinase Fgr oncogene homolog)
Sequence:
MESSDVELDLQRSVQAVLRELSTQAPALQSNQGMWRWSLHKKVERDPGKSPVLVRILLRELEKAESQDLRHVIIPLLHTVMYVLTKATGITEELYQRIYAFCTRLLTLPTPYCTVALDCAIRLKTEMAVPGTLYQRMVIAEQNLTNELYPYQERVFLFVDPELVSASVCSALLLEIEAAQAQQTPETCMRHVVSHALQAALGEACHAGALHRKLQASPRRTLEHYFHAVVAALEQMASEASPSREGHVERLEEIYCSLLGPAAGRCGGDLVQERPPSIPLPSPYITFHLWTGEEQLWKELVLFLRPRSQLRLSADLEVLDLQGLRPDRELARVSVLSTDSGIERDLPTGADELPAPGSPEMERAGLQRKGGIKKRAWPLDFLMPGSWDGPPGLHRRTGRPSGDGEMLPGVSRLHTARVLVLGDDRMLGRLAQAYHRLRKRETQKFCLTPRLSLQLYYIPVLAPEKPAASRQPELGELATFLGRVDPWYQSNVNTLCPAIHKLAEMPPSLDTSRTVDPFILDVITYYIRMGTQPIYFQIYTVKIFFSDLSQDPTEDIFLIELKVKIQDSKFPKDGFSPRRRGVAEGPGAELSLCYQKALLSHRPREVTVSLRATGLILKAIPASDTEVSGSSHCPLPAAPVTDHTCLNVNVTEVVKSSNLAGKSFSTVTNTFRTNNIQIQSRDQRLLTLSLDKDDQRTFRDVVRFEVAPCPEPCSGAQKSKAPWLNLHGQQEVEAIKAKPKPLLMPINTFSGIVQ
Protein: cDNA FLJ78762, highly similar to Homo sapiens zinc finger protein 224, mRNA (A8K8Y5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTFKEAMTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLSVGHQAFHRDTFHFLREEKIWMMKTAIQREGNSGDKIQTEMETVSEAGTHQEWSFQQIWEKIASDLTRSQDLVINSSQFSKEGDFPCQTEAGLSVIHTRQKSSQGNGYKPSFSDVSLFDFHQQLHSGEKSHMCDECGKNFCYISALRIHQRVHMGEKCYKCDVCGKEFSQSSHLQTHQRVHTGEKPFKCVECGKGFSRRSALNVHHKLHTGEKPYNCEECGKAFIHDSQLQEHQRIHTGEKPFKCDICGKSFCGRSRLNRHSMVHTAEKPFRCDTCDKSFRQRSALNSHRMIHTGEKPYKCEECGKGFICRRDLYTHHMVHTGEKPYNCKECGKSFRWASCLLKHQRVHSGEKPFKCEECGKGFYTNSQCYSHQRSHSGEKPYKCVECGKGYKRRLDLDFHQRVHTGEKLYNCKECGKSFSRAPCLLKHERLHSGEKPFQCEECGKRFTQNSHLHSHQRVHTGEKPYKCEKCGKGYNSKFNLDMHQKVHTGERPYNCKECGKSFGWASCLLKHQRLHSGEKPFKCEECGKRFTQNSQLHSHQRVHTGEKPYKCDECGKGFSWSSTRLTHQRRHSRETPLKCEQHGKNIVQNSFSEVQEKVHSVEKPYKCEDCGKGYNRRLNLDMHQRVHMGEKTWKCRECDMCFSQASSLRLHQNVHVGEKP
Protein: Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) (P05370)
Organism: Rattus norvegicus (Rat)
Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11413}. Membrane {ECO:0000250|UniProtKB:P11413}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11413}.
Interaction partners:
- Glucose-6-phosphate isomerase
- 6-phosphogluconolactonase
- GDH/6PGL endoplasmic bifunctional protein
- Hexokinase-3
- Hexokinase-2
- Cellular tumor antigen p53
- Glucose-6-phosphatase 3
- Phosphoglucomutase-1
- Uncharacterized protein.
- Glucose-6-phosphatase catalytic subunit 1
Sequence:
MAEQVALSRTQVCGILREELYQGDAFHQADTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPEDTFIVGYARSRLTVDDIRKQSEPFFKVTPEERPKLEEFFARNSYVAGQYDDPASYKHLNSHMNALHQGMQANRLFYLALPPTVYEAVTKNIQEICMSQTGWNRIIVEKPFGRDLQSSNQLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTDSDDVRDEKVKVLKCISEVETDNVVLGQYVGNPSGEGEATNGYLDDPTVPHGSTTATFAAAVLYVENERWDGVPFILRCGKALNERKAEVRLQFRDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHKIDREKPQPIPYVYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL
Protein: Ras-related protein Rap-1b (EC 3.6.5.2) (GTP-binding protein smg p21B) (Q62636)
Organism: Rattus norvegicus (Rat)
Function: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P61224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61224}. Cell junction {ECO:0000250|UniProtKB:P61224}. Note=May shuttle between plasma membrane and cytosol (By similarity). Presence of KRIT1 and CDH5 is required for its localization to the cell junction (By similarity). {ECO:0000250|UniProtKB:P61224}.
Interaction partners:
- Rap guanine nucleotide exchange factor 4
- RAS guanyl-releasing protein 2
- Krev interaction trapped protein 1
- Rap1 GTPase-activating protein
- Rap guanine nucleotide exchange factor 2
- Ral guanine nucleotide dissociation stimulator
- Rap guanine nucleotide exchange factor 3
- RAF proto-oncogene serine/threonine-protein kinase
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- RAS guanyl-releasing protein 1
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWSNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL
Protein: Acid-sensing ion channel 1 (A0A060D4V3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
DMLLSCYYRGMECSAEDFTVIFTRYGKCYTFNSGQDNRPLLVTMKGGMGNGLELMLDIQQDEYLPVWGETDETSFEAGIKVQIHTQDEPPFIDQLGFGVAPGFQTFVSCQEQRLTYLPPPWGDCKSTPIDSDFFSSYSLTACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVERDNDYCVCETPCNMTRFGKEMSFVKIPSKASAKYLAKKYNKTEQYIADNILVLDIFFEALNYETIEQTKAYEFAGLLGDIGGQMGLFIGASILTILELFDYLYEVIKYKLCRCSNKKHKRSNSNDRGAALSLEDIKRHTPCENLRTPGSYPANMLPHHPAQGNFEDFTC
Protein: Phosphatidylcholine:ceramide cholinephosphotransferase 1 (EC 2.7.8.27) (Protein Mob) (Sphingomyelin synthase 1) (Transmembrane protein 23) (Q7TSX5)
Organism: Rattus norvegicus (Rat)
Function: Major sphingomyelin synthase at the Golgi apparatus. Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER. The direction of the reaction depends on the levels of CER and DAG in Golgi membranes. Does not use free phosphorylcholine or CDP-choline as donor. Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting (By similarity). Plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86VZ5}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sphingomyelin phosphodiesterase
- Sphingomyelin phosphodiesterase 4
- Ceramide synthase 3
- Sphingomyelin phosphodiesterase 2
- Ceramide synthase 2
- Ceramide kinase
- Ceramide synthase 4
- Acid ceramidase
- Ceramide glucosyltransferase
- Neutral ceramidase
Sequence:
MLSASTMKEVVYWSPKKVADWLLENAMPEYCEPLGHFTGQDLINLTQEDFTKPPLCRVSSDNGQRLLDMIETLKMEHHIEAHKNGHANGHLSIGVDIPNPDGSFSIKIKPNGMPNGFRKEMIKIPMPEPERSQYPMEWGKTLLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFFDHFNRVQWAFSICEINGMILVGLWLFQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTTLPVPGMHFNCSPKLFGDWEAQVRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQVLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPLPWPVVHLSRQVKYSRLVNDT
Protein: Lymphocyte antigen 6 complex locus protein G6c (O95867)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000269|PubMed:17008713}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17008713}.
Interaction partners:
- Lymphocyte antigen 6 complex locus protein G5c
- Lymphocyte antigen 6 complex locus protein G6d
- Lymphocyte antigen 6 family member G6E
Sequence:
MKALMLLTLSVLLCWVSADIRCHSCYKVPVLGCVDRQSCRLEPGQQCLTTHAYLGKMWVFSNLRCGTPEEPCQEAFNQTNRKLGLTYNTTCCNKDNCNSAGPRPTPALGLVFLTSLAGLGLWLLH
Protein: Gem nuclear organelle associated protein 4 (I3L399)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFEACSQGPLNICEEMTILHGGFLLAEQLFHPKALAELTKSDWERVGRPIVEALREISSAAAHSQPFAWKKKALIIIWAKVLQPHPVTPSDTETRWQEDLFFSVGNMIPTINHTILFELLKSLEASGLFIQLLMALPTTICHAELERFLEHVTVDTSAEDVAFFLDVWWEVMKHKGHPQDPLLSQFSAMAHKYLPALDEFPHPPKRLRSDPDACPTMPLLAMLLRGLTQIQSRILGPGRKCCALANLADMLTVFALTEDDPQEVSATVYLDKLATVISVWNSDTQNPYHQQALAEK
Protein: Septum site-determining protein minD homolog, chloroplastic (AtMinD1) (Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 11) (Septum site-determining protein MinD1) (Q9MBA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with ARC3 and MCD1, regulates FtsZ ring positioning in chloroplasts in an ARC6-dependent manner. Calcium-dependent ATPase required for the correct placement of the plastid division site. Inhibits FtsZ filament and ring formation in the plastid. Mediates inhibition of plastid division. In cooperation with MINE1, prevents FtsZ ring formation anywhere outside of the mid-plastids.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:10801439, ECO:0000269|PubMed:11148270, ECO:0000269|PubMed:15126639, ECO:0000269|PubMed:16014621, ECO:0000269|PubMed:16146521, ECO:0000269|PubMed:19584524}; Peripheral membrane protein {ECO:0000269|PubMed:10801439, ECO:0000269|PubMed:11148270, ECO:0000269|PubMed:15126639, ECO:0000269|PubMed:16014621, ECO:0000269|PubMed:16146521, ECO:0000269|PubMed:19584524}. Note=Attached to membranes in punctate structures dispersed on the inner envelope and at the mid-chloroplast division site in an ATPase activity-dependent manner (PubMed:29967285). Also present at the chloroplast to a ring structure at the constriction site (PubMed:29967285). {ECO:0000269|PubMed:29967285}.
Interaction partners:
- Cell division topological specificity factor homolog, chloroplastic
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3
- Cell division protein FtsZ homolog 1, chloroplastic
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Plastid division protein CDP1, chloroplastic
- Protein MULTIPLE CHLOROPLAST DIVISION SITE 1
- Dynamin-like protein ARC5
- Plastid division protein PDV1
- Serine/Threonine-kinase RLCKVII protein
- Plastid division protein PDV2
Sequence:
MASLRLFSTNHQSLLLPSSLSQKTLISSPRFVNNPSRRSPIRSVLQFNRKPELAGETPRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSNFELLCISKPRSKLPMGFGGKALEWLVDALKTRPEGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVTGLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQAAWRLVEQDSMKAVMVEEEPKKRGFFSFFGG
Protein: N-acylglucosamine 2-epimerase (AGE) (EC 5.1.3.8) (GlcNAc 2-epimerase) (N-acetyl-D-glucosamine 2-epimerase) (Renin-binding protein) (RnBP) (P51607)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
Interaction partners:
- N-acetyl-D-glucosamine kinase
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
- N-acetylneuraminate lyase
- N-acetylneuraminate-9-phosphate synthase
- Beta-hexosaminidase subunit alpha
- Chitinase acidic-like 1
- Chitotriosidase-1
- Acidic mammalian chitinase
- Renin
Sequence:
MEKERETLQVWKQRVGQELDSVIAFWMEHSHDQEHGGFFTCLGRDGQVYDHLKYVWLQGRQVWMYCRLYRTFERFRRVELLDAAKAGGEFLLSYARVAPPGKKCAFVLTQDGRPVKVQRTIFSECFYTMAMNELWKVTGEMHYQREAVEMMDQIIHWVREDPAGLGRPQLSGTLATEPMAVPMMLLNLVEQLGEEDEEMTDKYAELGDWCAHRILQHVQRDGQVVLENVSEDGKELPGCLGRHQNPGHTLEAGWFLLQYALRKGDPKLQRHIIDKFLLLPFHSGWDPEHGGLFYFQDADDLCPTQLEWNMKLWWPHTEAMIAFLMGYRDSGDPALLNLFYQVAEYTFHQFRDPEYGEWFGYLNQEGKVALTIKGGPFKGCFHVPRCLAMCEQILGALLQRLGPAPLGSLPAVPTREGSK
Protein: Phosphoserine phosphatase SerB1 (PSP) (PSPase) (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) (P9WGJ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Likely catalyzes the dephosphorylation of O-phospho-L-serine into L-serine.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphoserine aminotransferase
- Sulfate transport system permease protein CysT
- Sulfate/thiosulfate import ATP-binding protein CysA
- Uncharacterized protein Rv0508
- UPF0336 protein Rv0504c
- Cyclopropane mycolic acid synthase 2
- Phosphoserine phosphatase SerB2
- D-3-phosphoglycerate dehydrogenase
Sequence:
MMVSSHLGSPDQAGHVDLASPADPPPPDASASHSPVDMPAPVAAAGSDRQPPIDLTAAAFFDVDNTLVQGSSAVHFGRGLAARHYFTYRDVLGFLYAQAKFQLLGKENSNDVAAGRRKALAFIEGRSVAELVALGEEIYDEIIADKIWDGTRELTQMHLDAGQQVWLITATPYELAATIARRLGLTGALGTVAESVDGIFTGRLVGEILHGTGKAHAVRSLAIREGLNLKRCTAYSDSYNDVPMLSLVGTAVAINPDARLRSLARERGWEIRDFRIARKAARIGVPSALALGAAGGALAALASRRQSR
Protein: Deoxyribose-phosphate aldolase (DERA) (EC 4.1.2.4) (2-deoxy-D-ribose 5-phosphate aldolase) (Phosphodeoxyriboaldolase) (Deoxyriboaldolase) (P0A6L0)
Organism: Escherichia coli (strain K12)
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Can also catalyze the double aldol condensation of three acetaldehyde molecules, leading to the formation of 2,4,6-trideoxyhexose (Ref.5).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000305}.
Interaction partners:
- Phosphopentomutase
- Thymidine phosphorylase
- Uncharacterized protein YhfW
- Purine nucleoside phosphorylase DeoD-type
- Triosephosphate isomerase
- Transketolase 1
- Fructose-bisphosphate aldolase class 2
- Transketolase 2
- Transaldolase B
- Ribokinase
Sequence:
MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTLKEQGTPEIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIKAGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSLLASLLKALGHGDGKSASSY
Protein: Nitric oxide synthase (EC 1.14.13.39) (Q90WQ8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MKLLQDDETKLSHQTKPNKWETRANRCPFSIPVRNVKDGSSLKDMLHHQAVKNQPCTSKVCEGSVMTPKALLRGPKVSTLEILPQAIDLINQYYKSFKIPKIEHHLARLEEITMEIDSTGTYQLTVEELAFGARQAWRNAPRCIGRIQWSNLQLFDARKCKTTQEMFQFLCEHLQFATNGGNLRSAITVFPPRKEDGHDFRVWNSQLLKYAGYQMPDGSIQGDPSSVEFTKICIQLGWKPQYGLFDVLPLVLQVNGEDPDLYEIPPHLILEVSMEHPQHKWFQDLGLKWYALPAVSNMLMEIGGLEFPACPFNGWYMGTEIGVRDFCDYQRYNILEEVGRRMGLETHKLSSLWKDQALVTINVAVIYSFQKNKVTITDHHSAAESFMKHLETEFRLRGGCPADWAWLVPPMSGSLTPIFHQEMVNYILSPFFYYQPDPWMTHVWRNGEMCLKKQQISFKAVARAALFSSTLMSRVLAKRVRCTVLYATETGKSQTLAQRLNSMLNGAFNSRLLCMEDYNFSDMEQESLLVVVTSTFGNGDSPGNGESFKKQLFSLQYLRNKLRYCVFGLGSRMYPQFCAFAHAVDAKLEELGAERVTPTGEGDELNGQEEAFSAWALTALKDAYKEFKIQGQLSLQLPGAERFCEAWDPLRHRVAEESCPQDRITALSAIHSKTVFPMKLKSKHNLQSPHSSRSTILVELERERSAEVMNFAPGDHVGVFPGNLPQLVAGILKFLPHTPPTNQCLRLEYRSDTCRDDEKNWQTVGRIPACPLSQALTYFLDVTTPPSQNLLHKLSQLAKQEGHRQRLLTLAKDSQEYTTWKMFRVPNFLEVLEEFPSLELSAAFLLSQLPLLKPRLYSISSSPQLHPNELHLTLTVLNYHTQDGQGPLHHGVCSTWLDTIKKGDLVPCFIYSSGGFHLPAEPSTPVILVGAGSGIAPFRSFWQQRLHDMKHPEFSESPMSLVFGCQSSETDHLYKEETLEMRRRGVLKSVTNAYSRQPGLPKVYVQDVLRERMAEEVLSVLHQKEGHFYVCGGVNMAQGVTLAVQEILSSQLGITLTQAGEYLTQLKIQKRYHEDIFGAQFQK
Protein: Tegument protein UL35 (F5HE12)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Plays important role in immediate-early gene expression through interaction with UL82. Forms nuclear bodies in host nucleus, independently of PML. In turn, UL35 nuclear bodies associate with and remodel PML bodies. Through interaction with host DCAF1, causes cells to accumulate in the G2 phase of the cell cycle by inducing a DNA damage response. Regulates viral assembly by controlling the localization of the essential gB through regulation of a retrograde transport pathway. This modulation occurs via binding and inhibition of host sorting nexin 5/SNX5. Also plays a role in the inhibition of pattern recognition receptor-mediated type I interferon signaling at the level of TBK1.
Subcellular location: [Isoform UL35]: Virion tegument {ECO:0000250|UniProtKB:P16766}. Host nucleus {ECO:0000250|UniProtKB:P16766}. Host cytoplasm {ECO:0000250|UniProtKB:P16766}. Note=Found in nuclear bodies. {ECO:0000250|UniProtKB:P16766}.; SUBCELLULAR LOCATION: [Isoform UL35A]: Host nucleus {ECO:0000250|UniProtKB:P16766}. Host cytoplasm {ECO:0000250|UniProtKB:P16766}.
Interaction partners:
Sequence:
MAQGSRAPSGPPLPVLPVDDWLNFRVDLFGDEHRRLLLEMLTQGCSNFVGLLNFGVPSPVYALEALVDFQVRNAFMKVKPVAQEIIRICILANHYRNSRDVLRDLRTQLDVLYSEPLKTRLLRGLIRLCRAAQTGVKPEDISVHLGADDVTFGVLKRALVRLHRVRDALGLRASPEAEARYPRLTTYNLLFHPPPFTTVEAVDLCAENLSDVTQRRNRPLRCLTSIKRPGSRTLEDALNDMYLLLTLRHLQLRHALELQMMQDWVVERCNRLCDALYFCYTQAPETRQTFVTLVRGLELARQHSSPAFQPMLYNLLQLLTQLHEANVYLCPGYLHFSAYKLLKKIQSVSDARERGEFGDEDEEQENDGEPREAQLDLEADPTAREGELFFFSKNLYGNGEVFRVPEQPSRYLRRRMFVERPETLQIFYNFHEGKITTETYHLQRIYSMMIEGASRQTGLTPKRFMELLDRAPLGQESEPEITEHRDLFADVFRRPVTDAASSSSASSSSSSASPNSVSLPSARSSSTRTTTPASTYTSAGTSSTTGLLLSSSSLSGSHGISSADLEQPPRQRRRMVSVTLFSPYSVAYSHHRRHRRRRSPPPAPRGPAHTRFQGPDSMPSTSYGSDVEDPRDDLAENLRHL
Protein: Ovalbumin-related protein X (R9TNA6)
Organism: Gallus gallus gallus
Interaction partners:
Sequence:
MFFYNTDFRMGSISAANAEFCFDVFNELKVQHTNENILYSPLSIIVALAMVYMGARGNTEYQMEKALHFDSIAGLGGSTQTKVQKPKCGKSVNIHLLFKELLSDITASKANYSLRIANRLYAEKSRPILPIYLKCVKKLYRAGLETVNFKTASDQARQLINSWVEKQTEGQIKDLLVSSSTDLDTTLVLVNAIYFKGMWKTAFNAEDTREMPFHVTKEESKPVQMMCMNNSFNVATLPAEKMKILELPFASGDLSMLVLLPDEVSGLERIEKTINFEKLTEWTNPNTMEKRRVKVYLPQMKIEEKYNLTSVLMALGMTDLFIPSANLTGISSAESLKISQAVHGAFMELSEDGIEMAGSTGVIEDIKHSPELEQFRADHPFLFLIKHNPTNTIVYFGRYWSP
Protein: Period circadian regulator 1 (Period homolog 1 (Drosophila), isoform CRA_b) (J3QSH9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGPLEGADGGGDPRPGESFCPGGVPSPGPPQHRPCPGPSLADDTDANSNGSSGNESNGHESRGASQRSSHSSSSGNGKDSALLETTESSKSTNSQSPSPPSSSIAYSLLSASSEQDNPSTSGCSSEQSARARTQKELMTALRELKLRLPPERRGKGRSGTLATLQYALACVKQVQANQEYYQQWSLEEGEPCSMDMSTYTLEELEHITSEYTLQNQDTFSVAVSFLTGRIVYISEQAAVLLRCKRDVFRGTRFSELLAPQDVGVFYGSTAPSRLPTWGTGASAGSGLRDFTQEKSVFCRIRGGPDRDPGPRYQPFRLTPYVTKIRVSDGAPAQPCCLLIAERIHSGYEAPRIPPDKRIFTTRHTPSCLFQDVDERAAPLLGYLPQDLLGAPVLLFLHPEDRPLMLAIHKKILQLAGQPFDHSPIRFCARNGEYVTMDTSWAGFVHPWSRKVAFVLGRHKVRTAPLNEDVFTPPAPSPAPSLDTDIQELSEQIHRLLLQPVHSPSPTGLCGVGAVTSPGPLHSPGSSSDSNGGDAEGPGPPAPLQARSRPRPFPANPQTQSWRRVLLPSRPH
Protein: Catalase (EC 1.11.1.6) (A2Q7T0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MRHFWLLPAVAGIAGAQCPYLSGEMSFTQEQDNAGDTIEVTEQPIDNTLYVNDTGSYMTTDFGTPISDQTSLKAGPRGPTLLEDFIFRQKLQRFDHERVPERVVHARGAGAYGTFKSYADWSNVTAADFLSANDKETPMFCRFSTVVGFRGSVDTARDVHGHACQFYTDEGNYDIVGINFAPFFIQDAIQFPDLVHAIKPMPNNEIPQAATAHTSAWDFFSQQSTALHSALWLMSGNGIPRSFRHMNGYGVHSFRFVAANGTSKVVRYRWKSQQGVASLVWDEAQAAAGKNSDYHRQDLYNAIANGHYPKYELQAQIMDEADMLRFGFDLLDPTKLVPEEVVPYTPLGMMELNANPTNYFAEVEQAGFQPGHVVPGIDFTDDPLLQGRLFSYLDTQLTRHGGPNFEQIPVNRPRKPVHNNNRDGFGQQQIPTNNWAYTPNSMSNGYPMQANQTQGHGFFTAPYRYASGHLVRQTSPTFNDHWSQPAMFWNSLIPAEQQMVVNAIVFQNSKVNSPHVRKNVVNQLNMVNNNLAVRVARGLGLDEPSPNPTYYTSNKTSNVGTFGKPLLSIEGLQVGFLASNSHPESIKQGQAMAAQFSAAGVDLNIVSEAYADGVNTTYALSDAIDFDALIIADGVQSLFASPALANQMNSTATSTLYPPARPFQILVDSFRYGKPVAAVGSGSVALKNAGIDSSRSGVYTGSSETTEKIAKEVLEGLYTFRFVDRFALDE
Protein: Cyclin-related 2 family protein (Q75J86)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Ankyrin repeat-containing protein
- F-box domain-containing protein
- Uncharacterized protein
Sequence:
MSKVYSKSQTVSPGKPQNIFVTALPSSVSAPSLLSLQKPNNGAGSHRKQRQNSGSSKNRPNLPLDQIKSTERKNSGNKSNNNNNKNRKYSKNNSNVNSNNINSSSIVIKCEEQQQQQQQQQQQQQQQQQQQQQQQQDGFLKSQEFPNLFKNKLYLKDDISSPSSSSSTSSPSCLSSSSSSTFSQSEIAENKDDINNNNCNNTNGNFEEEEEEEEKNKVEQQSIEEETFIESSFEETKEVVEEVPFEEQFEILPISIGEETLKEYTSFLSVLSELIVDMYNDDDKSSTSSQSSSSSSSSSAPSSPKPIKNNDNNTTTTTTTTATTTTTSKTATSSLSTIEKFQVFNVDQIPEISIEAYIERVFKYLPFGTDIFIFSTIYLDRLIQWNQEIQISPLNIHRLFMASIIVASKFHNDKALNNRYYAQVGGISLFEMNQLEIHFLLLLNWKLHIDPEIFDAFKTSIQSKIDILDMKIRKLSNNGNINNESNKENIVIKTTEEKVKNSEIHINSNNNDCNNNNNNATVTTNPTPNPNPTITTTSTTTTTTTTTIPTPSTQSNNNNCNNSTKRYVTLVETDKNNSKPKTKYNSSNKSTNNGGTSQFSRILNNRGSKNVSYHHPNYLTYPLAAPQTNYQPQQQQQQTYYQPPHHQQQYYQQQQYYSNYQYNQQLSYYQQQQQHYDDYYQQQQIPIPPQPQNYIYQQPYHSTSSTSSTNIYIGKSGTPSSPNMNDICGGVSESYDSQIPSSFGSSSGSGSVGSCTSSSIGSTTAGSASQYQPHSWQNAYYYGGVATSQFSYHTPTYQ