wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclic GMP-AMP phosphodiesterase SMPDL3A (2',3'-cGAMP phosphodiesterase SMPDL3A) (EC 3.1.4.-) (Acid sphingomyelinase-like phosphodiesterase 3a) (ASM-like phosphodiesterase 3a) (EC 3.6.1.15) (P70158)
Organism: Mus musculus (Mouse)
Function: Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP. Has in vitro activity with p-nitrophenyl-TMP. Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates. Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine. Does not have sphingomyelin phosphodiesterase activity (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:25288789, ECO:0000269|PubMed:26095358, ECO:0000269|PubMed:26792860}.
Interaction partners:
- BMP/retinoic acid-inducible neural-specific protein 1
Sequence:
MALLGNFLCCLLVAWLCGPGLGVPLAPADRAPAVGQFWHVTDLHLDPTYHITDDRTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSPPHVPVPELSTGTVIKVITNMTMTVQNLFPNLQVFPALGNHDYWPQDQLPIVTSKVYSAVADLWKPWLGEEAISTLKKGGFYSQKVASNPGLRIISLNTNLYYGPNIMTLNKTDPANQFEWLENTLNSSLWNKEKVYIIAHVPVGYLPYATDTPAIRQYYNEKLLDIFRRYSSVIAGQFYGHTHRDSLMVLSDKNGNPLNSVFVAPAVTPVKGVLQKETNNPGVRLFQYKPGDYTLLDMVQYYLNLTEANLKGESNWTLEYVLTQAYSVADLQPKSLYALVQQFATKDSKQFLKYYHYYFVSYDSSATCDQHCKTLQVCAIMNLDSMSYDDCLKQHL
Protein: Numb-related protein 1 (CKA1) (Protein kinase C adapter 1) (Q9XTY6)
Organism: Caenorhabditis elegans
Function: Involved in the tethering and targeting of pkc-3 to modulate the intracellular distribution of the kinase. The complex formed with pkc-3 complexes are likely to be involved in assembly, maintenance, and/or regulation of protein complexes that execute asymmetric and/or polarized cell functions.
Subcellular location: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Note=Expressed at the inner surface of the plasma membrane at the cell periphery (which includes a region corresponding to plasma membrane and/or actin cortical cytoskeleton) in early embryos. Tightly associated with organelles and/or cytoskeletal structures with some diffuse expression in the cytoplasm. Differentially routed to lateral junctions between polarized cells.
Interaction partners:
- Protein kinase C-like 3
- Protein lin-12
- AP-2 complex subunit alpha
- Intersectin-1
- Serine/threonine-protein kinase sel-5
- Nicastrin
- Actin
- Cell division control protein 42 homolog
- RNA-binding protein Musashi homolog 1
- Dynamin
Sequence:
MSASQGNVFTRGLSRISRRKKKTKSIQNSLVSEQQPSFDAAIVPMPIPNDKSSIFSKGMDRLRRSLRLPKKRRDRSHDRHLSPDVTGGSKTEQWQPDEGAVRTGTCCFNVKYLGSVEVYESRGMQVCEGALKSLKASRRKPVKAVLYVSGDGLRVVDQGNSRGLLVDQTIEKVSFCAPDRQTDKGFAYICRDGASRRWMCHGFLATKETGERLSHAVGCAFSICLEKKKRRDEETAQVNVQSAQESTSSTPPKDIFHPNWEDNTSEGTSTQNPSNSRSNLAYQSFRKHVSIEDRYLDPQSVIINEVPASNHMDEIRRISKPRPTGNPALFLRQGSLRAPPDMPSSSDQFKRNMSLRTVSNNPTERSPEKKSFGTQLYNEPIYEGDEDPLGLGITPPVVTKTSGSLSNNGLDGINLNWKSIPAPVHQMQQHNANGDFVAAWPQNTIEKPTVGPLDKLQKQFEDIKLISISSGENTPTTRSKADEWLDDVLRVSMSMSPTSPSSDPPSTSSYSVLPKSGPPPAHAPPPLPVRQAVSNGSPSIYQQQLQQANSTRNSPAGINWNSSPNPMKISQPPAKPVDPFDVQWSRLAVNNTH
Protein: DNA (cytosine-5-)-methyltransferase (EC 2.1.1.37) (A0A1B9GEF8)
Organism: Kwoniella bestiolae CBS 10118
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- YDG domain-containing protein
- Proliferating cell nuclear antigen
- SET domain-containing protein
- ubiquitinyl hydrolase 1
- Polyubiquitin
- dTDP-4-dehydrorhamnose reductase
- Histone H3
- Histone H3-like centromeric protein CSE4
- Histone H3
- Histone H3
Sequence:
MSPLTEIIEIGDSDSDIESIDITSRSNSTSTSRSICEYNESGRKRKRDDEIENISSDEEEVEIRSQLRELSVQVEASNLKDKQKASYISPPAHPCPPPATASKRHKSHSANRPMSSPARQHGLSTSRASKAGKAQLTWLKEDAITPARAIKRSTYKVNGFEEDCVRIYREGFHHDGDEFTVDDAILLPHSPPLYILIRSIFTLKFDDPVIHDRHLVHVHLFKPPVSGGRKGELFLRNAQCQDIPIKQILKGKKLDFELIGGIRRRGRGDSEYFCEFVDQSSLSTIREPKFQDRFHNCDSCLSRHQKHRFDHPYISNDTLHFGDDEYHISDFISIDSKIRGQPFLFGHIHGWRKGDGEIMVRVRRLRRFSEVAGEKYEGFTSNRQLVVTDKYEDHPVKLIMGKVYVLPDDKNTRSFHPHITFWCSERMTDPHNSTTRVVLQKPLRSCSTCLEREEQRHKDLQDCMKACQFPAADYYSGAGGFILPGLDIFDWVSAADTEKVACQTLHHLKRRAPALTVHYGKVSDVYNYTTSRDSPIGNSKAFPAPGTVFLMTGGPPCQGHSRVNHANNPTAESLQNKDPRNDELWVMLAEAFRLKPFVIIIENVSAFKDDKGGSGRSEAEENYGRAAMKKLSQNGYSCRLGIIDSRGFGTPQNRLRTFILGVRVGIPLPDFPAPSHANPKTTATVFKGDKSGVIKPFYLGQRATPGTGIHPAVTIQDAISDLPAFEYLPPPGIARVPRRPQIPAFNGGRNDQGNGTKVGFPHRVPYGSEPTNEYQKEKRGDQPTVPDHFTSYVTDGAHKIIFTSAREPKPQGCDRRALLSEGFSTLLTNSSPGQKGTAVIHPSQDRKFTIAERKRAMGWPDWHRLAGTPLEQDKLTGNGVCYESVQAIYMALVKEIILPWWIEAGRPTEGVFQKFVEDHQ
Protein: Krueppel-like factor 11 (Transforming growth factor-beta-inducible early growth response protein 2) (TGFB-inducible early growth response protein 2) (TIEG-2) (O14901)
Organism: Homo sapiens (Human)
Function: Transcription factor. Activates the epsilon- and gamma-globin gene promoters and, to a much lower degree, the beta-globin gene and represses promoters containing SP1-like binding inhibiting cell growth. Represses transcription of SMAD7 which enhances TGF-beta signaling (By similarity). Induces apoptosis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9748269}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Tyrosine-protein kinase Blk
- Paired box protein Pax-4
- Neurogenic differentiation factor 1
- Hepatocyte nuclear factor 1-alpha
Sequence:
MHTPDFAGPDDARAVDIMDICESILERKRHDSERSTCSILEQTDMEAVEALVCMSSWGQRSQKGDLLRIRPLTPVSDSGDVTTTVHMDAATPELPKDFHSLSTLCITPPQSPDLVEPSTRTPVSPQVTDSKACTATDVLQSSAVVARALSGGAERGLLGLEPVPSSPCRAKGTSVIRHTGESPAACFPTIQTPDCRLSDSREGEEQLLGHFETLQDTHLTDSLLSTNLVSCQPCLHKSGGLLLTDKGQQAGWPGAVQTCSPKNYENDLPRKTTPLISVSVPAPPVLCQMIPVTGQSSMLPAFLKPPPQLSVGTVRPILAQAAPAPQPVFVGPAVPQGAVMLVLPQGALPPPAPCAANVMAAGNTKLLPLAPAPVFITSSQNCVPQVDFSRRRNYVCSFPGCRKTYFKSSHLKAHLRTHTGEKPFNCSWDGCDKKFARSDELSRHRRTHTGEKKFVCPVCDRRFMRSDHLTKHARRHMTTKKIPGWQAEVGKLNRIASAESPGSPLVSMPASA
Protein: Cytochrome bc1 complex cytochrome c subunit (EC 7.1.1.8) (Cytochrome bc1 reductase complex subunit QcrC) (Ubiquinol--cytochrome c reductase cytochrome c subunit) (P9WP35)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Cytochrome b subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of ubiquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis.
Subcellular location: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Probable cytochrome c oxidase subunit 1
- Uncharacterized protein Rv2876
- Cytochrome bc1 complex cytochrome b subunit
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Probable cytochrome c oxidase polypeptide 4
- Probable cytochrome c oxidase subunit 3
- Putative lipoprotein LpqE
- Elongation factor Tu
- Superoxide dismutase
Sequence:
MTKLGFTRSGGSKSGRTRRRLRRRLSGGVLLLIALTIAGGLAAVLTPTPQVAVADESSSALLRTGKQLFDTSCVSCHGANLQGVPDHGPSLIGVGEAAVYFQVSTGRMPAMRGEAQAPRKDPIFDEAQIDAIGAYVQANGGGPTVVRNPDGSIATQSLRGNDLGRGGDLFRLNCASCHNFTGKGGALSSGKYAPDLAPANEQQILTAMLTGPQNMPKFSNRQLSFEAKKDIIAYVKVATEARQPGGYLLGGFGPAPEGMAMWIIGMVAAIGLALWIGARS
Protein: Protein phosphatase (EC 3.1.3.16) (Q9W3R1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO10752p1
- AT18705p
- GH19655p
- Serine/threonine-protein phosphatase alpha-3 isoform
- CG6036 protein
Sequence:
MDVETSLDIEEMRRRIQQGINRCCEQLLEIAMILTHKGGQVLNRLKGASFPELAQNSENIGNGSMSENQNQRLDPMTSAQYTTLGFGNFDGEGDYLRQKNKINIQLPRLVSVTCGFAKDHIRYPEYNRGKFGEDAWFMSSSPQACIMGVADGVGGWRNYGVDPGKFSMTLMRSCERMSHAPDFKPNRPEILLERAYFDLLDQKCPIVGSCTACILALKRDDSTLYAANIGDSGFLVVRSGKVVCRSQEQQHQFNTPYQLASPPPGYDFDAVSDGPESADTIQFPMQLGDVILLATDGVYDNVPESFLVEVLTEMSGISNPVRLQMAANTVALMARTLSFSPKHDSPFSQNARKHDIDAWGGKPDDITVLLASVV
Protein: Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (O95749)
Organism: Homo sapiens (Human)
Function: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32403198}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32403198}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:32403198}.
Interaction partners:
- Farnesyl pyrophosphate synthase
- Diphosphomevalonate decarboxylase
- Isopentenyl-diphosphate Delta-isomerase 1
- Squalene synthase
- Isopentenyl-diphosphate delta-isomerase 2
- Dehydrodolichyl diphosphate synthase complex subunit DHDDS
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- All trans-polyprenyl-diphosphate synthase PDSS1
- Protein farnesyltransferase subunit beta
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
Sequence:
MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE
Protein: Nuclear pore complex protein Nup214 (214 kDa nucleoporin) (DNup214) (Nucleoporin Nup214) (Q9W1X4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Part of the nuclear pore complex. Serves as a docking site in the receptor-mediated import of substrates across the nuclear pore complex including emb, RanGAP and phosphorylated Mad. Protects mbo/Nup88 from proteasomal degradation at the nuclear pore. Together with mbo/Nup88, sequesters emb in the cytoplasm and thereby attenuates nuclear export signal (NES)-mediated nuclear export. Together with mbo/Nup88, required for the nuclear import of the Rel family transcription factors dorsal (dl) and Dorsal-related immunity factor (Dif) and the activation of an immune response.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:20547758}. Nucleus membrane {ECO:0000269|PubMed:17032737}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:20547758}. Note=Localization to the nucleus membrane depends on mbo/Nup88. {ECO:0000269|PubMed:17032737}.
Interaction partners:
- Nuclear pore complex protein Nup153
- Exportin-1
- Nuclear pore complex protein Nup88
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup133
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup154
- Nuclear pore complex protein Nup75
Sequence:
MAQNAPDCEDTQDFQFKLHHKIVAFKKCGEPRSNVNLLAVSSSRGLLFAGSPTQPELKVIIVKDLVNAKSTAQQPQARLVPLPSIPNYIACSSDGNLLAVNHTQNGTSLLSIYAVLSFMTPDVRPVYNIRLAAEDHVHGVQLLWNPVLPNSLAVVLSNGALAMYALKEGGNFEMHSLDKNQQVKCGCWSPKGKQIVLGFPGGTVKQFKPDLTLAKTLLCPPNIHDAPFDTIAIQWLSTFQFAVIFLQHGEDCSPSLYILNAPKAGAPSYINYYDICYSMNGPRNHQFVFSHVPQWNLLLVVSANGVEVGIMRSTEAGDTPAWQQLTLLDEARIEMPLSEDKDETFPLGFAFDTSTTHQLTINEKKLQTMPMVHVLSSDGELLSFNFLNVLPTAVSVCSPPPPVADTSGQFKPLNMLLASEEEEQPAWAASPSKAPAATPAASSDISFAFTPNTVTSTPAPSKDKQPSLFSGFGAAAAKAPAPQLSFGTAPTSSPVSFGAPTTNAAKPTTPFGGFGTQATTTAMGSMFSASGANAFGGMALNKPAIASVTPRTAAPGSTVPATPASAPANKPLYTVPLTFTPVDTKPATSAPPQIADESLKPDDTEPIIKDMIALQIEAFSKDIQKQKEQTKELLKGIAAPSALRAYAKRLDDLQELNEQAKDVEFELDVQGLRQGLNEAYAIVAECRGKLEIYRKPEITRLMNSSSCDPSGRRMLARLQSYVAANEAQLRLAQQHVDLQWEQFQDVVRRNSKSRMHMPCLEGIYQRLTRLQNLTSNQRIVQNNIKSKLKERGLLQAALLDQEKSRTRTNEAVDTLTDSILTMSLSQVVDSNAAKLTRERLQKIRNIVQLQKINVICPQRPDRVGLKSEVILETKRRAEQIKRAAAKPATANKYTQAAVAPPSPPDVAPTPAVAPMPQATVTVAPPLPKPMPSIPSVVEKPGVPTHPTTPVATPFSFSQSIPFVKTSTVTPTTNTVTPGEAAKPGLSIFGGSTISSFSFGGGAAKSALSFGTGSPAVAAPTPKPNPLSAVEKPTPEPTKPKEQKAAESKEFKAVQPETEESKVPQKPKAETENKSFGFGGFTGTGGTVGNTSSSPFSFGGLGSSLGFGGTAAAVPKSEPSSTATTSVATSASTAPFGIFSAALAKPSNSEPITTVTSNTTTITSKPTNVIASSSVTDAPSVTTTNAVTSSTDPIGGLFSSVTICKPNTPADTTKPANIFGGGLSAGSFSFGGTIDASKGLFGSTKPVATAPTSVTEANNKTDPISTTPSAISTTTATTTVSSPAVVPAAVTAAVPATSSTTVTSSTAVPGSAFSFSNAFSTLSAGGAAAPTTSASAPLAAKSPTATSTGNNSSNSVFGGGFAVATSTAAPVASPFQSAAKSPVSSANIFGSIPKAETSVFGGATTAPSNTTAAATPDAPPAGLFASAAISNPSPFGSPTTRAPASGGNIFGQAVKPSVFGQPAQAGDSGGSIFGGGSASTPFGSSSIFGGGNTQGAVGAPAAGSTSIFGQKVFGQSSAAAPAAGGNIFSNPVGSPQASPFGGGGNSIFGSPATAPPASGGSIFGGGSSSGGFGSFTQTTPAQGGFGGGFGQGGGGSVAQTGFGSPQAPQQQTTTPGGFGAKPVFGGSPAFGASPTFGGGATFGSPKGFGGFGGASPVASPPPFGAAAKPAQGNIFETLGGQESGLSFGNLAQTGNSNAQKPAFGGSSFMNYR
Protein: Dynein regulatory complex subunit 4 (Growth arrest-specific protein 11) (GAS-11) (Growth arrest-specific protein 8) (GAS-8) (O95995)
Organism: Homo sapiens (Human)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dual roles at both the primary (or non-motile) cilia to regulate hedgehog signaling and in motile cilia to coordinate cilia movement. Required for proper motile cilia functioning. Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by facilitating the trafficking of SMO into the cilium and the stimulation of SMO activity in a GRK2-dependent manner (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10969087}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:16643277, ECO:0000269|PubMed:26387594}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q60779}. Golgi apparatus {ECO:0000269|PubMed:16643277}. Cell projection, cilium {ECO:0000269|PubMed:27120127}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q7XJ96}. Note=Associates with microtubules (PubMed:10969087). Localized to the cytoplasm of round spermatids, the tails of elongating spermatids, and mature spermatid tail bundles protruding into the lumen, and in the flagellum of epididymal spermatozoa (By similarity). {ECO:0000250|UniProtKB:Q60779, ECO:0000269|PubMed:10969087}.
Interaction partners:
- Dynein regulatory complex subunit 2
- Dynein regulatory complex protein 1
- Axonemal dynein light intermediate polypeptide 1
- Dynein regulatory complex subunit 7
- Glia-derived nexin
- Protein smoothened
- Dynein axonemal intermediate chain 2
- Dynein regulatory complex subunit 5
- Radial spoke head 1 homolog
- Coiled-coil domain-containing protein 39
Sequence:
MAPKKKGKKGKAKGTPIVDGLAPEDMSKEQVEEHVSRIREELDREREERNYFQLERDKIHTFWEITRRQLEEKKAELRNKDREMEEAEERHQVEIKVYKQKVKHLLYEHQNNLTEMKAEGTVVMKLAQKEHRIQESVLRKDMRALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKMLRDELDLRRKTELHEVEERKNGQIHTLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILLCTKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEKKEVQFNEVLAASNLDPAALTLVSRKLEDVLESKNSTIKDLQYELAQVCKAHNDLLRTYEAKLLAFGIPLDNVGFKPLETAVIGQTLGQGPAGLVGTPT
Protein: O-glycoside alpha-1,2-mannosyltransferase homolog 4 (EC 2.4.1.-) (O94565)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable mannosyltransferase involved in O-glycosylation of cell wall and secreted proteins. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLGWNKHVFFSESRINFRCLLRKKLKKRCPLSARFVLVLLLIVLIFILKMGYKQLIYKLNHPPLRRIDERNDPLFSNGCKNVHLEAQLHPRMNATFVMLARNSDLPGVVSSINSLEKHFNRHFNYPYTFLNDEPFDEKFKETILKLTSANVEFGTLEKDTFGFPGNVDVDAAREAIASQGDRGIMYGDTESYHHMCRFFSGFFYKHPLLLKYQWYWRVEPDVAFTCDISYDPFYYMEENGKIYGYVVALKELEDTVPNLFRYTSAYRRNNNLTSNMWKFFLDAPKKENYDISRKDPTVGLSFSSHLNAMIDSSYSAETSSMEGESYNMCHFWSNFEIANFKFFRNEQYENFFRTMDATGGFWTERWGDAPFHSLAAGLFLSKEQVHYFRDLGYRHSDIHHCGQSLGCNCECIPELSEIESTSGGCVTQWVNLIGDGFLDE
Protein: 4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) (4-(phosphohydroxy)-L-threonine dehydrogenase) (P19624)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}.
Interaction partners:
- Pyridoxine 5'-phosphate synthase
- Ribosomal RNA small subunit methyltransferase A
- Phosphoserine aminotransferase
- Protein ApaG
- Bis
- Chaperone SurA
- Erythronate-4-phosphate dehydrogenase
- Threonine synthase
- Pyridoxine/pyridoxamine 5'-phosphate oxidase
- DNA gyrase subunit B
Sequence:
MVKTQRVVITPGEPAGIGPDLVVQLAQREWPVELVVCADATLLTNRAAMLGLPLTLRPYSPNSPAQPQTAGTLTLLPVALRAPVTAGQLAVENGHYVVETLARACDGCLNGEFAALITGPVHKGVINDAGIPFTGHTEFFEERSQAKKVVMMLATEELRVALATTHLPLRDIADAITPALLHEVIAILHHDLRTKFGIAEPRILVCGLNPHAGEGGHMGTEEIDTIIPVLNELRAQGMKLNGPLPADTLFQPKYLDNADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTALELAGRGKADVGSFITALNLAIKMIVNTQ
Protein: Anp1p (C8Z6V8)
Organism: Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast)
Interaction partners:
Sequence:
MKYNNRKLSFNPTTVSIAGTLLTVFFLTRLVLSFFSISLFQLVTFQGIFKPYVPDFKNTPSVEFYDLRNYQGNKDGWQQGDRILFCVPLRDASEHLPMFFNHLNTMTYPHNLIDLSFLVSDSSDNTMGVLLSNLQMAQSQQDKSKRFGNIEIYEKDFGQIIGQSFSDRHGFGAQGPRRKLMARARNWLGSVALKPYHSWVYWRDVDVETIPTTIMEDLMHHDKDVIVPNVWRPLPDWLGNIQPYDLNSWKESEGGLQLADSLDEDAVIVEGYPEYATWRPHLAYMRDPNGNPEDEMELDGIGGVSILAKAKVFRTGSHFPAFSFEKHAETEAFGRLSRRMNYNVIGLPHYVIWHIYEPSSDDLKHMAWMAEEEKRKLEEERIREFYNKIWEIGFEDVRDEWNEERDSILKNIDSTLNNKVTVDWSEEGDGSELVDSKGDFVSPNNQQQQQQQQQQQQQQQQQQQQQLDGNLQGKPLDDNDKNKKKHPKEVPLDFDPDRN
Protein: Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (1-alkyl-2-acetylglycerophosphocholine esterase) (EC 3.1.1.47) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase) (P04180)
Organism: Homo sapiens (Human)
Function: Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines. Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms. Catalyzes the hydrolysis of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor or PAF) to 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF). Also catalyzes the transfer of the acetate group from PAF to 1-hexadecanoyl-sn-glycero-3-phosphocholine forming lyso-PAF. Catalyzes the esterification of (24S)-hydroxycholesterol (24(S)OH-C), also known as cerebrosterol to produce 24(S)OH-C monoesters.
Subcellular location: Secreted {ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:8016111, ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma (PubMed:10222237, PubMed:3458198, PubMed:8820107). Produced in astrocytes and secreted into cerebral spinal fluid (CSF) (PubMed:10222237). {ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:8820107}.
Interaction partners:
- Apolipoprotein A-I
- Cholesteryl ester transfer protein
- Apolipoprotein B-100
- Apolipoprotein A-II
- Apolipoprotein C-I
- Serum paraoxonase/arylesterase 1
- Apolipoprotein C-III
- Apolipoprotein E
- Phospholipid transfer protein
- Phosphatidylethanolamine N-methyltransferase
Sequence:
MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLGAYRQGPPASPTASPEPPPPE
Protein: NAC domain-containing protein 82 (ANAC082) (Protein VND-INTERACTING 1) (Q9FY82)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that binds specific DNA sequences on the promoter regions of target genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- 18S rRNA
- MJK13.9 protein family protein)
Sequence:
MGKTQLAPGFRFHPTDVELVRYYLKRKILGKKLLVDAIAEVDIYKFEPPDLPDMSFIRSGDLKWHFFCPREKKYASGVRANRATECGYWKTTGKERPVLCNSEVVGKIKTLVYHFGKSPRGERTDWVMHEYRLDDKVLTQMNVPQDTYVVCVLFKKDGPGPRNGAQYGAPFKEEDWSDEEVRTDVPSTSNPTNLLEPSKETTLALTAPDDSNKDCFGGMISESCVSDFLPATTNTTSELPHPSDAATTPMSTAPLAETVQTPNNDDLYSMLDLFDDDEEFLGFNNNEVRYDPGVSAPVCLEEEGIFNGLPELSSMPRTASYDLVENSELYLELQDLTAPLNPQTGLQDLTAPFNPQTGLQDLTAPFNHQTGLQDHTAPFNPQTGLQDHTAPFNHQTGLQDLTAPFNPQTGLQDLTAPFNPQTGLHDLTSPFNPQTGLQDLTAPLNPQTGNRNDPRSSSFLYNQGHFDFSGGNDDDPYGFSASMRHRPKM
Protein: Chemokine XC receptor 1 (G-protein coupled receptor 5) (Lymphotactin receptor) (XC chemokine receptor 1) (P46094)
Organism: Homo sapiens (Human)
Function: Receptor for chemokines SCYC1 and SCYC2. Subsequently transduces a signal by increasing the intracellular calcium ions level. Receptor for XCL1/Lymphotactin.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Cytokine SCM-1 beta
- Lymphotactin
- C-C motif chemokine 8
- C-C motif chemokine 5
- Guanine nucleotide-binding protein G
- C-C motif chemokine 3
- C-X-C motif chemokine 9
- Stromal cell-derived factor 1
- Metallophosphoesterase 1
- Interleukin-8
Sequence:
MESSGNPESTTFFYYDLQSQPCENQAWVFATLATTVLYCLVFLLSLVGNSLVLWVLVKYESLESLTNIFILNLCLSDLVFACLLPVWISPYHWGWVLGDFLCKLLNMIFSISLYSSIFFLTIMTIHRYLSVVSPLSTLRVPTLRCRVLVTMAVWVASILSSILDTIFHKVLSSGCDYSELTWYLTSVYQHNLFFLLSLGIILFCYVEILRTLFRSRSKRRHRTVKLIFAIVVAYFLSWGPYNFTLFLQTLFRTQIIRSCEAKQQLEYALLICRNLAFSHCCFNPVLYVFVGVKFRTHLKHVLRQFWFCRLQAPSPASIPHSPGAFAYEGASFY
Protein: Calpain-10 (EC 3.4.22.-) (Calcium-activated neutral proteinase 10) (CANP 10) (Q9ESK3)
Organism: Mus musculus (Mouse)
Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin-stimulated glucose uptake (By similarity).
Interaction partners:
- Calpain small subunit 1
- Calpastatin
- Calpain small subunit 2
- Aminopeptidase RNPEPL1
Sequence:
MRAVRAETPARELFRDAAFPASDSSLFYNLSTPLAQFREDITWRRPQEICATPQLFPDNPWEGQVKQGLLGDCWFLCACAALQKSQHLLDQVFPPGQPGWSDQKYQGFFTCRIWQFGHWEEVTIDDRLPCLAGRLCFSRCQREDVFWLPLLEKAYAKVHGSYEHLWAGQVADALVDLTGSLAERWSLKDVTKASGQQDRPSGGEHRTCRQLLHLKDRCLISCSVLSPRAGARELGEFHAFIISDLQELRSQTGQGILLLRIHNPWGRRCWQGLWREGGEGWNQVEPAKESELLAQLQEGEFWVEEEEFLREFDEVTIGYPVTEAGHLQSLHTERVLCHTRTLPGAWVTGQSAGGCRNNSCFPCNPKFWLRLLEPSEVCVAVLQRPRRRLVGQTRALAGASPAPVNLPGKDYQAVGLHIWKVEKRKISLPRVLSAPPVAGTACHAYDREIHLRCELSPGYYLAVPSTFLKDVPGQFLLRVFSTGKISLSAVRLATKGASPGTALPAGEWETVQLQGCWRAGQTAGGSRNFASYPCNPCLPFSVPEGAGPRYIRITLQQHCRLSDSQLHPIGFHVFQVPADGENQDACSLLLQEPLLSCVPHRYAQEVSRLCLLSVGNYRIVPSTYLPDTEGTFTVTIATRIDRQSIHSQEMLGQLLQEVSFMAVMKA