wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase) (Q9HV49)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- Dihydrofolate synthase/folylpolyglutamate synthase
- 7,8-dihydroneopterin aldolase
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
- Phosphoglucosamine mutase
- Aminodeoxychorismate lyase
- GTP cyclohydrolase 1 2
- GTP cyclohydrolase 1 1
- ATP-dependent zinc metalloprotease FtsH
- Dihydrofolate reductase
Sequence:
MSNPQYPTRLPCGSRVLDLARPHVMGILNVTPDSFSDGGRYDRLDDALRHAERMVLEGATLIDVGGESTRPGARSVSPTEELERVAPVVERIARELDVVISVDTSTPAVMRETARLGAGLINDVRSLQRDGALDAAVDSGLAVCLMHMRGEPQTMQDAPAYQDVVAEVGAFLQERVDACVAAGIDRERLLLDPGFGFAKTLEHNLVLFRHLQALHGLGLPLLVGVSRKSMIGKVLGREVDERLYGSLALAALALAKGARIIRVHDVAATVDVMRMISAVEMAD
Protein: SH3KBP1-binding protein 1 (SETA-binding protein 1) (Q6P7W2)
Organism: Mus musculus (Mouse)
Function: Inhibits CBL-SH3KBP1 complex mediated down-regulation of EGFR signaling by sequestration of SH3KBP1. Binds to SH3KBP1 and prevents its interaction with CBL and inhibits translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q8TBC3}.
Interaction partners:
- Galectin-4
Sequence:
MAVATTAVEGVPSRGAPGEVIHLNVGGKRFSTSRQTLTWIPDSFFSSLLSGRISTLKDETGAIFIDRDPTVFAPILNFLRTKELDPRGVHGSSLLHEAQFYGLTPLVRRLQVREELDRSSCGNVLFNGYLPPPVFPVKRRNRHSLVGPQQIGGRPAPVRRSNTMPPNLGNAGLLGRMLDERAPPSPSGQPEEPGMVRLVCGHHNWIAVAYTHFLVCYRLKEASGWQLAFSSPRLDWPIERLALAARVLGGAPGEHDKMVAAATGSEILLWALQAQGGGSEIGVFHLGVPVEALFFVGNQLIATSHTGRIGVWNAVTKHWQVQEVQPITSYDAAGSFLLLGCSNGSIYYVDVQKFPLRMKDNDLLVSELYRDPAEDGVTALSVYLTPKTSDSGNWIEIAYGTSSGVVRVIVQHPETVGSGPQLFQTFSVHRSPVTKIMLSEKHLISVCADNNHVRTWSVTRFRGMISTQPGSTPLASFKILALESVDGLGGCSAGNDIGPYGERDDQQVFIQKVVPNASQLFVRLSSTGQRVCSVRSVDGSPTTAFTVLECEGSRRLGSRPRRYLLTGQANGSLAMWDLTTAMDGLGQTPAGGLTEEELMDQLEQCELSPLASSRGSFPSPSPRTSLTSLHSASSNTSLYGPRGSPSPPQAEARRRGAGSFVDRCQELARGAPELRWPPTPAPRPSTSLGNPLTALKKTLNETSF
Protein: Endoplasmic reticulum transmembrane protein 3 (Q07451)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in invertase secretion.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein SCS2
- Endoplasmic reticulum transmembrane protein 1
- Dynamin-related protein DNM1
- Transcriptional repressor OPI1
- Mitochondrial fission 1 protein
- Protein CASP
- Protein translocation protein SEC63
- Protein SSP120
- ER-derived vesicles protein ERV41
- ER-derived vesicles protein ERV46
Sequence:
MSLYYTLVFAILVVEIFMFSILALPIPSRYRRPLTLLLLKPFKSSTVQVAIKCVLGFILLLFIDCINRVYSIDKELQLSSASQNNGAIIAQDRIEVLSRKFFAQRNMYLTGITLFLTFVVVRTFGLVIELLTMKDIYRASPPVASSDVKKNDSVTAEAAAQSGASKDDHGDEKNFELLKKIQDIDDEIARLKEKSESLQEEIN
Protein: Lysophosphatidic acid receptor 2 (LPA receptor 2) (LPA-2) (Lysophosphatidic acid receptor Edg-4) (Q9HBW0)
Organism: Homo sapiens (Human)
Function: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway. Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation.
Subcellular location: Cell surface {ECO:0000269|PubMed:19306925}. Cell membrane {ECO:0000269|PubMed:19306925}; Multi-pass membrane protein {ECO:0000269|PubMed:19306925}. Note=Prior to LPA treatment found predominantly at the cell surface but in the presence of LPA colocalizes with RALA in the endocytic vesicles.
Interaction partners:
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 5
- Lysophosphatidic acid receptor 4
- Lysophosphatidic acid receptor 6
- Guanine nucleotide-binding protein subunit alpha-12
- Na
- Lysophosphatidic acid receptor 1
- Lysophosphatidic acid receptor 3
- Guanine nucleotide-binding protein subunit alpha-13
- Proteinase-activated receptor 1
Sequence:
MGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASNRRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVATLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSRMAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLVKTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDAEMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
Protein: Dye-decolorizing peroxidase YfeX (EC 1.11.1.-) (Porphyrinogen oxidase) (P76536)
Organism: Escherichia coli (strain K12)
Function: Has both general peroxidase activity and dye-decolorizing activity. Can catalyze the oxidation of both protoporphyrinogen IX and coproporphyrinogen III to their corresponding porphyrins. Also efficiently decolorizes the dyes alizarin red and Cibacron blue F3GA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19564607}.
Interaction partners:
- Deferrochelatase
- UTP pyrophosphatase
- Iron uptake system component EfeO
Sequence:
MSQVQSGILPEHCRAAIWIEANVKGEVDALRAASKTFADKLATFEAKFPDAHLGAVVAFGNNTWRALSGGVGAEELKDFPGYGKGLAPTTQFDVLIHILSLRHDVNFSVAQAAMEAFGDCIEVKEEIHGFRWVEERDLSGFVDGTENPAGEETRREVAVIKDGVDAGGSYVFVQRWEHNLKQLNRMSVHDQEMVIGRTKEANEEIDGDERPETSHLTRVDLKEDGKGLKIVRQSLPYGTASGTHGLYFCAYCARLHNIEQQLLSMFGDTDGKRDAMLRFTKPVTGGYYFAPSLDKLMAL
Protein: Cytosolic arginine sensor for mTORC1 subunit 1 (Cellular arginine sensor for mTORC1 protein 1) (GATS-like protein 3) (Q8WTX7)
Organism: Homo sapiens (Human)
Function: Functions as an intracellular arginine sensor within the amino acid-sensing branch of the TORC1 signaling pathway. As a homodimer or a heterodimer with CASTOR2, binds and inhibits the GATOR subcomplex GATOR2 and thereby mTORC1. Binding of arginine to CASTOR1 allosterically disrupts the interaction of CASTOR1-containing dimers with GATOR2 which can in turn activate mTORC1 and the TORC1 signaling pathway.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26972053}.
Interaction partners:
- GATOR2 complex protein MIOS
- Cytosolic arginine sensor for mTORC1 subunit 2
- GATOR2 complex protein WDR24
- GATOR2 complex protein WDR59
- Nucleoporin SEH1
- Protein SEC13 homolog
- Neutral amino acid transporter 9
- Zinc finger C2HC domain-containing protein 1A
- Ras-related GTP-binding protein C
- Ras-related GTP-binding protein A
Sequence:
MELHILEHRVRVLSVARPGLWLYTHPLIKLLFLPRRSRCKFFSLTETPEDYTLMVDEEGFKELPPSEFLQVAEATWLVLNVSSHSGAAVQAAGVTKIARSVIAPLAEHHVSVLMLSTYQTDFILVREQDLSVVIHTLAQEFDIYREVGGEPVPVTRDDSSNGFPRTQHGPSPTVHPIQSPQNRFCVLTLDPETLPAIATTLIDVLFYSHSTPKEAASSSPEPSSITFFAFSLIEGYISIVMDAETQKKFPSDLLLTSSSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAADISAYYISTFNFDHALVPEDGIGSVIEVLQRRQEGLAS
Protein: DNA double-strand break repair nuclease NurA (EC 3.1.-.-) (Q97WH1)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Involved in DNA double-strand break (DSB) repair. Acts probably with HerA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Processes linear dsDNA probes with 3' or 5' single-stranded overhangs or blunt ends.
Interaction partners:
- DNA double-strand break repair helicase HerA
- DNA repair and recombination protein RadA
- DNA double-strand break repair Rad50 ATPase
- DNA double-strand break repair protein Mre11
Sequence:
MIRKIYDKLVESHNEIKNQIYNIANYLKQEIQDKVNEYWNEYVINHEQSETCKFVAIDGGSFGRPMRIGIVYAVGAESVIGDNKGVKTLSEDGQIGIFKPGNDAQERISLLMEALELSLALRDGSKGDYILMDGSLSKKIGNKVDIQQFSDEELKLIRNVDLNGIISIKDERKMRDLLMLLNQFLVSKIIEEYDGNVLWISKVSRGRDLFGTDYPDITVLELFTEKRGFSKLIIKNIDIEKISEIPEIEVLRKMEYTTFYTRLDNGKRVIRVDIVGRVDEKIVKEIMDRLSGVSIKGYPFPLLKAHMDVRFSAMDREKIIKLVGSKLHKDIEWWPSQFY
Protein: GTPase ERA-like, chloroplastic (GTP-binding protein Era-like) (Q8VZ74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nuclear genome-encoded probable GTPase involved in ribosome biogenesis in chloroplasts. Plays a role in 16S rRNA maturation in plastids and may contribute to the assembly of the small (30S) ribosomal subunit.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000250|UniProtKB:K7UTH7}.
Interaction partners:
- Small ribosomal subunit protein mS29
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- At1g64880
- Transmembrane protein
- Pentatricopeptide repeat-containing protein At1g02060
- Octanoyltransferase LIP2p, chloroplastic
- Ethylene-responsive transcription factor ERF015
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein uS9m
- EMBRYO DEFECTIVE 3147
Sequence:
MAVSPHISPTLSRYKFFSTSVVENPNFSPYRIYSRRRVTKSHLQAHNSTTSYGRTELSSSKKLWIRQRSFSEMEVEQAQLEDDEEQVEIDIVDEASLLSLSMKPDRNMALLDDYEMEELGHTPNTHHRSGYVAVVGMPNVGKSTLSNQMIGQKISIVTDKPQTTRHRILGICSSPEYQMILYDTPGVIEKKMHRLDTMMMKNVRDAAINADCVVILVDACKTPTNIEEVLKEGLGDLEKKPPMLLVMNKKDLIKPGEIAKKLEWYEKFTDVDEVIPVSAKYGHGIEDVKEWILSKLPFGPPYYPKDIVSEHPERFFVSEIVREKIFMQYRNEVPYACQVNVLSYKTRPAAKDFIQVEVVVDKNSQKIILIGKEGKALKTLATAARLDIEDFLQKKVFLEVEVKVKENWRQDEGLLKYYGYGGQIRAM
Protein: Cell division control protein 16 (P36618)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a dual role in the cell cycle. In mitosis, it is involved in maintenance of cdc2 kinase activity. It is subsequently required for regulation of septum formation. Could be involved in maintenance of cdc2 kinase activity by preventing, directly or indirectly, the degradation of cyclin or the dephosphorylation of 'Thr-167' of cdc2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Septum-promoting GTP-binding protein 1
- Serine/threonine-protein kinase plo1
- Protein byr4
- Cell division control protein 7
- Tyrosine-protein phosphatase CDC14 homolog
- Septation initiation network scaffold protein cdc11
- Probable E3 ubiquitin-protein ligase dma1
- Protein phosphatase PP2A regulatory subunit B
- Spindle assembly checkpoint protein bub3
- UBA domain-containing protein Mud1
Sequence:
MPSIDCKRLQKLAPKSPENQSKCISRLRYMVMLDQVESDEGGNSSTRPYVWAVLLNAPPRNADEYIRYVRQGPSPMAQKIQNDVSRTLVVESQFHSRVSQSSLSRLLNAYVWKRGALYVQGMNVLASPFLYACKSENQAFQFFDRLLQNECPLYVLPNIDGVHRGAKLLDKCLEVLDHRLYTYLLSKGLTAKIYALPSILTLSACTAPLSEALTIWDFLFAYGIHLNILCVIAQMFIFREQLIDHPSPMTLLRTFPPLNAKNIMKITILLISKLPPELYNLLARHAWDSEAGVLIDRLT
Protein: Transcription activator GLK1 (GBF'S PRO-RICH REGION-INTERACTING factor 1) (Golden2-like protein 1) (AtGLK1) (Q9SIV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that functions with GLK2 to promote chloroplast development. Acts as an activator of nuclear photosynthetic genes involved in chlorophyll biosynthesis, light harvesting, and electron transport. Acts in a cell-autonomous manner to coordinate and maintain the photosynthetic apparatus within individual cells. May function in photosynthetic capacity optimization by integrating responses to variable environmental and endogenous cues. Prevents premature senescence.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9FFH0}.
Interaction partners:
- NAC domain-containing protein 92
- Pentatricopeptide repeat-containing protein GUN1, chloroplastic
- Tetrapyrrole-binding protein, chloroplastic
- Magnesium-chelatase subunit ChlH, chloroplastic
- Protochlorophyllide reductase B, chloroplastic
- Transcription factor HY5
- GATA transcription factor 21
- Glutamyl-tRNA reductase 1, chloroplastic
- RNA polymerase sigma factor sigF, chloroplastic
- Putative GATA transcription factor 22
Sequence:
MLALSPATRDGCDGASEFLDTSCGFTIINPEEEEEFPDFADHGDLLDIIDFDDIFGVAGDVLPDLEIDPEILSGDFSNHMNASSTITTTSDKTDSQGETTKGSSGKGEEVVSKRDDVAAETVTYDGDSDRKRKYSSSASSKNNRISNNEGKRKVKVDWTPELHRRFVEAVEQLGVDKAVPSRILELMGVHCLTRHNVASHLQKYRSHRKHLLAREAEAANWTRKRHIYGVDTGANLNGRTKNGWLAPAPTLGFPPPPPVAVAPPPVHHHHFRPLHVWGHPTVDQSIMPHVWPKHLPPPSTAMPNPPFWVSDSPYWHPMHNGTTPYLPTVATRFRAPPVAGIPHALPPHHTMYKPNLGFGGARPPVDLHPSKESVDAAIGDVLTRPWLPLPLGLNPPAVDGVMTELHRHGVSEVPPTASCA
Protein: alpha-1,2-Mannosidase (EC 3.2.1.-) (Q8MS36)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MSTTSSESFVRGQRLMLIFLVAMCIVVACVLSTETTMPTQNMSNKERAELREEARDMFYHAYNAYMQNAYPADELMPLSCKGRYRGVTPSRGDMDDILGNFSMTLVDTLDTLVLLGDFTEFDHAVKLVIREVQFDSDIIVSVFETNIRMVGGLLSAHILAEYLQKHADTMHWYKGELLEMSRELGYRLLPAFNTSTGIPHARVNLRLGMKDPMLKKSRETCTACAGTILLEFAALSRLTGDPIFEVRAHAAMDALWKLRHRGSDLMGTVLNVHSGDWVRRDSGVGAGIDSYYEYLFKSYVLLGDDKYLARFNRHYNAVMKYVSEGPMLLDVLMHRPHAKSKNFMDSLLAFWPGLQVLSGDLKPAVQTHEMLYQVMQMHTFIPEAFTVDFQIHWGQHPLRPEFIESTYFLYRATGDHHYLQVGKKALKTLQQHAKVSCGYAAVNDVRTGKHEDRMDSFVLSETIKYLFLLFSDPQDLIINVDEFVFTTEAHLLPLSIAQLGNATFSFRQTDEHNVLDFMRTCPSSNRLFPEKVRKPLRNFITGSCPRTTAGKRLSALDFQASNADHLRAVYDMGITMVSVGDRSQGKVRLFHSFYNAKSHEEGEMGLQFMQEMLELTKMQSINQLAQLQAVAYATDENSQDWIALMAGPSHFSPELTGDQFVEGDVILAKPLRACDESLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSGETQPMFAMSGDGKDDVLIPVVFMYSMEFGKLSAVMQRRKQPLRVRVMQMVEFKRWQLAKEQRQNQTASVAQKPEKEL
Protein: Lamin-1 (Ce-lamin) (CeLam-1) (Q21443)
Organism: Caenorhabditis elegans
Function: Major component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane. Provides a framework for the nuclear envelope and probably also interacts with chromatin. Essential to maintain the shape and integrity of the nucleus, and for DNA replication. Involved in spatial organization of nuclear pore complexes. It is not a target for ced-3 during apoptosis, suggesting that lamin cleavage is not essential for apoptosis in C.elegans.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:16950114}. Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:12490171, ECO:0000269|PubMed:25057012}; Lipid-anchor {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12490171}; Nucleoplasmic side {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12490171}. Note=Remains in the nuclear envelope until late anaphase in early embryos. Depends on mel-28 for nuclear envelope localization after mitosis. {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:16950114}.
Interaction partners:
- LEM protein 2
- Barrier-to-autointegration factor 1
- Emerin homolog 1
- Sun domain-containing protein 1
- Nuclear migration and anchoring protein unc-84
- Protein mel-28
- Small ribosomal subunit protein uS5
- Nuclear pore complex protein Nup98-Nup96
- Transmembrane protein 201 homolog
- Nucleoporin NUP35
Sequence:
MSSRKGTRSSRIVTLERSANSSLSNNGGGDDSFGSTLLETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQVDMTTYAKQINDEYQSKLQDQIEEMRAQFKNNLHQNKTAFEDAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRSELDTLKRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQEAPQNTSVHHVSFSSGGASAQRGVKRRRVVDVNGEDQDIDYLNRRSKLNKETVGPVGIDEVDEEGKWVRVANNSEEEQSIGGYKLVVKAGNKEASFQFSSRMKLAPHASATVWSADAGAVHHPPEVYVMKKQQWPIGDNPSARLEDSEGDTVSSITVEFSESSDPSDPADRCSIM
Protein: Solute carrier family 23 member 2 (Na(+)/L-ascorbic acid transporter 2) (Sodium-dependent vitamin C transporter 2) (Q9WTW8)
Organism: Rattus norvegicus (Rat)
Function: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10331392}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UGH3}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Uridine monophosphate synthetase, isoform CRA_a.
Sequence:
MMGVGKNTSKSVEVGGSTEGKYEEEAKRPDFFTLPVVINGGATSSGEQDNEDTELMAIYTTENGIAEKSSLAETLDSTGSLDPQRSDMIYTIEDVPPWYLCIFLGLQHYLTCFSGTIAVPFLLADAMCVGDDQWATSQLIGTIFFCVGITTLLQTTFGCRLPLFQASAFAFLAPARAILSLDKWKCNTTEITVANGTAELLEHIWHPRIQEIQGAIIMSSLIEVVIGLLGLPGALLRYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKFPLPIYKSKKGWTAYKLQLFKMFPIILAILVSWLLCFIFTVTDVFPSNSTDYGYYARTDARKGVLLVAPWFKVPYPFQWGMPTVSAAGVIGMLSAVVASIIESIGDYYACARLSCAPPPPIHAINRGIFVEGLSCVLDGVFGTGNGSTSSSPNIGVLGITKVGSRRVIQYGAALMLGLGMIGKFSALFASLPDPVLGALFCTLFGMITAVGLSNLQFIDLNSSRNLFVLGFSIFFGLVLPSYLRQNPLVTGITGIDQVLNVLLTTAMFVGGCVAFILDNTIPGTPEERGIKKWKKGVSKGNKSLDGMESYNLPFGMNIIKKYRCFSYLPISPTFAGYTWKGFGKSENRRSSDKDSQATV
Protein: UDP-2,3-diacylglucosamine pyrophosphatase LpxI (EC 3.6.1.54) (UDP-2,3-diacylglucosamine hydrolase LpxI) (Q9A716)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to form 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the beta-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Can functionally complement lpxH deficiency in E.coli. Cannot use CDP-diacylglycerol as substrate.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:23042606}; Peripheral membrane protein {ECO:0000305|PubMed:23042606}; Cytoplasmic side {ECO:0000305|PubMed:23042606}.
Interaction partners:
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- UDP-3-O-acylglucosamine N-acyltransferase
- Lipid-A-disaccharide synthase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Tetraacyldisaccharide 4'-kinase
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- Outer membrane protein assembly factor BamA
- 3-deoxy-D-manno-octulosonic acid transferase
- Lipid A biosynthesis acyltransferase
- Oxidoreductase, Gfo/Idh/MocA family
Sequence:
MRKLGLIAGGGALPVELASHCEAAGRAFAVMRLRSFADPSLDRYPGADVGIGEFGKIFKALRAEGCDVVCFAGNVSRPDFSALMPDARGLKVLPSLIVAARKGDDALLRRVLDEFEKEGFEIEGAHEVMGEMTLPRGRLGKVSPAPEHMADIDKALDVAREIGRLDIGQGAVVCEGLVLAVEAQEGTDAMLRRVADLPEAIRGRAERRLGVLAKAPKPIQETRVDLPTIGVATIHRAARAGLAGIVGEAGRLLVVDREAVIAAADDLGLFVLGVDPQERP
Protein: 5-deoxyribose kinase (EC 2.7.1.-) (5-deoxyribose disposal kinase) (Methylthioribose kinase) (MTR kinase) (EC 2.7.1.100) (P0DTQ2)
Organism: Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73)
Function: Catalyzes the ATP-dependent phosphorylation of 5-deoxyribose into 5-deoxy-alpha-D-ribose 1-phosphate, as part of a 5-deoxyribose salvage pathway that recycles this toxic radical SAM enzyme by-product to mainstream metabolites. Is also able to catalyze the phosphorylation of 5-methylthioribose into methylthioribose 1-phosphate, but this enzyme may not function in methionine salvage in B.thuringiensis since it exists a paralog (MtnK) present in the methionine salvage pathway cluster. Does not act on 5-deoxyribulose, 2-deoxyribose, ribose, fucose, fructose, fructose 6-phosphate, and glucose.
Interaction partners:
Sequence:
MSKFTKYFLMEASDVIAYVKEKLSKFEHAKGLKCKEIGDGNLNYVFRVWDKKENMSVIVKQAGDTARISDEFKLSTNRIRIESDVLQLENELAPGLVPKVYLFDSVMNCCVMEDLSNHTILRTALINHQIFPQLADDLTTFMVNTLLLTSDVVMNHKEKKELVKNYINPELCEITEDLVYSEPFTNHNKRNELFPLNEGWIREHIYSDKELRMEVAKRKFSFMTNAQALLHGDLHTGSVFVRDDSTKVIDPEFAFYGPMGYDVGNVMANLMFAWVNADATMPPGAEKDTYMDWLQTTMVEVIDLFKKKFLDAWDIHVTEIMAKEEGFNEVYLQSVLEDTAAVTGLELIRRIVGLAKVKDITCIENEEARARAEQICLKVAKSFILRANQYRTGRSFVETLKEQSMHYAE
Protein: Nucleoside-diphosphatase mig-23 (NDPase) (EC 3.6.1.6) (Abnormal cell migration protein 23) (Q21815)
Organism: Caenorhabditis elegans
Function: Seems to be able to hydrolyze ADP, UDP and GDP. Supports mig-17 glycosylation and surface expression, which is required for proper migration of distal tip cells during gonad morphogenesis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14688791, ECO:0000269|PubMed:16354716}; Multi-pass membrane protein {ECO:0000269|PubMed:14688791, ECO:0000269|PubMed:16354716}.
Interaction partners:
- Nucleoside-diphosphatase uda-1
- Ribonucleoside-diphosphate reductase large subunit
- Ribonucleoside-diphosphate reductase small chain
- Uridine kinase
- Inosine triphosphate pyrophosphatase
- UMP-CMP kinase 1
- UMP-CMP kinase 2
- AMP deaminase
- guanylate kinase
- Adenylosuccinate synthetase
Sequence:
MRVSLRFTILAVSAMIFFPVIVFIYVVEAHTSPKVIADDQERSYGVICDAGSTGTRLFVYNWISTSDSELIQIEPVIYDNKPVMKKISPGLSTFGTKPAQAAEYLRPLMELAERHIPEEKRPYTPVFIFATAGMRLIPDEQKEAVLKNLRNKLPKITSMQVLKEHIRIIEGKWEGIYSWIAVNYALGKFNKTATLDFPGTSPAHARQKTVGMIDMGGASAQIAFELPDTDSFSSINVENINLGCREDDSLFKYKLFVTTFLGYGVNEGIRKYEHMLLSKLKDQNGTVIQDDCMPLNLHKTVTLENGENFVRRGTGNWNTCSNEVKKLLNPESSSEVCKAEAAKCYFGAVPAPSIPLSNIEMYGFSEYWYSTHDVLGLGGQYDAENIAKKTQQYCSKRWSTIQAESKKQLYPRADEERLRTQCFKSAWITSVLHDGFSVDKTHNKFQSVSTIAGQEVQWALGAMIYHMRFFPLRDSSRNLIVKETHSSSESLWAPLFFLSAVFCLFVLVCAKEQSVLCFDDKRRSSFGMSRSQYSYKMLKENRTSSSFLENFA
Protein: Histone H2B type 1-M (H2B 291B) (P10854)
Organism: Mus musculus (Mouse)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H3.2
- Histone H3.1
- Histone H3.3
- Histone H4
- Plasminogen
- Histone H2AX
- Breast cancer type 1 susceptibility protein homolog
- Histone deacetylase 1
- Histone H2A type 2-C
- Histone H2A type 1-K
Sequence:
MPEPTKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Trophoblast glycoprotein a (A0A0R4ITS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Protein Wnt
- Protein Wnt
Sequence:
MFARGRCAVVLGLLCAAAVSAGALVCPTGCECSEAALTVKCVSKDLRDIPSGIPGYTRNLFITGNHISQIGPESFQGLENVTNLSLSNNRISEVKSHTFSSLRSLRSLDLSNNQLAVIHPEAFTVQSRMLRELNLSRALYNHSSVMDLATSLRWSSLSDLLVLDLSSNGLVFLPSGIFCHLVGLRRLQLGNNSIVSIHNGTFTGLDHLQELDLTHNALRTLREEALKELEQLHSARLHLADNPFTCTCDIEPFAAWLNGSRGQVVDIEGLTCAFPVALHNTSLLTVGDLELGCHKAGDSDNLALQTSYVFLGLVLGFVGLMFLFVLYLNRKDIKKRIYDMRDACREVWEGYHYRYEIDSDPRLSQVSSTADV
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FL46)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Transcription factor
- Cell division control protein 42
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase STE20
- Candida glabrata strain CBS138 chromosome L complete sequence
- M-phase inducer phosphatase
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MSLSREDSVFLTKLAEQAERYEEMVENMKDVASAGQELSVEERNLLSVAYKNVIGARRASWRIVSSIEQKEESKENSEHQIKLIKDYRAKIEAELTKISDDILSVLDKHLIPSASSGESKVFYYKMKGDYHRYLAEFSQGDVRENATKASLDAYQKASEIATTELPPTHPIRLGLALNFSVFYYEIQNSPDKACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMSEADDQKNEESK
Protein: Protein ERD1 (P16151)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the retention of luminal endoplasmic reticulum proteins, affects glycoprotein processing in the Golgi apparatus.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Cystine transporter
- Protein MEH1
- ER lumen protein-retaining receptor
- Phospholipid-transporting ATPase NEO1
- Conserved oligomeric Golgi complex subunit 5
- Mannan polymerase complexes subunit MNN9
Sequence:
MEKSESNSEGLYLQNILNVPPPQRFIVLIILALWIWTWILKFFLHSNLDVSQVILTRVPHDIRPGYTLQQLHRTARNFALKITRIIIPFHFATVFLFEFMNIIEGPLKNIILIVYFLPLIQCVTIFWFLLKECQIIKYCTRRCLLIESSPRSLRNTYILISDTLTSFAKPLIDFTLFTSLIFREPFTHFDLSVALLPVLVRLLQCLREYRLLHEATLLFNALKYSCNLPILFCTWRSRVYEGSINEERLHHVQRWFMLINSSYTLFWDVRMDWSLDSLTSLRSRSKSAVTLKKKMYHSAILVDFLLRFWWLWVYLSQNLKLVAADSDYIFFQGEMQYFEVIRRGIWVVFKLDAEYYIKFASK