wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphocholine transferase AnkX (PC transferase) (EC 2.7.1.-) (Ankyrin repeat-containing protein X) (Q5ZXN6)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as a phosphocholine transferase by mediating the addition of phosphocholine to Ser residues of host RAB1 (RAB1A, RAB1B or RAB1C) and RAB35, leading to displacement of GDP dissociation inhibitors (GDI). Phosphocholination of target proteins also impairs accessibility to GTPase effector LepB. Can act on both GDP-bound and GTP-bound Rab proteins.
Subcellular location: Secreted {ECO:0000269|PubMed:22158903}. Host cytoplasm {ECO:0000269|PubMed:22158903}. Note=Translocated into the host cell via the type IV secretion system (T4SS).
Interaction partners:
- Chaperone protein DnaK
- Polyketide synthase, type I
- Serine carboxypeptidase
- Uridine kinase
- Coenzyme F390 synthetase
- histidine kinase
- Probable sphingosine-1-phosphate lyase
- Uncharacterized protein
- Probable thermolabile hemolysin
- Endo-1,4-beta-xylanase-like
Sequence:
MVKIMPNLPGLYFLQAYPSEEIWRLFVDGRFWSKENGWRGYESREPGCLNAALESLCSIALQVEKSGEEFELSVDLIKRIHKKCGKKVEELQEKNPGELRTDEPVSFGIPAGRASIKGIEEFLSLVFLTEGGAEFGPGKAGPFGPRFDKNYFKNLNPEQIPDLAKQIYFDMCKYGHSNTNHFYLAVMKNVDVYLEKITQSYNKEIKTAETLDEKLKIIVKHIRMYEVLHPFRDANGRTFVNNLLNILLMQQGLPPATFYEPNVFDLYSAEELVVVVKEAIFNTVEIIEQSKRKTPITLYGYHSSLEEQTKFRDMLDSPSYEKIKHMDFSDLNPEKLHLKTQKCLSSLNEQYPLHRGAIYLSDPGEIKLLLSNRNESQINQQIEQGAPPIYVGKTPAHLAVISGNMAMLDELIAKKADLSLQDYDGKTALHYAAECGNMQIMGKILKVVLSQEDAIKVLNIKDNHGKTAFHYAAEFGTPELISALTTTEVIQINEPDNSGSSAITLAYKNHKLKIFDELLNSGADISDELLDAIWARKDKETLGKIIAKNEKILLNKEAFRIAISLGSVSLVKKFLRAGVDIDIPLTKDKATPLMLSINSGNPKLVSYLLKKGANTRLTDTSGNSVLHYVFYSKAENREALANIITEKDKKLINQPNANGNPPLYNAVVVNDLKMATILLEMGARVDFEDRLGNNILHSAMRRCDLPIILDIVKKDSTLLHKRNSERRNPFHQALHEMHTFPSSKETEEIHFMNLSDLLLKEGVDLNKKDIKGKTILDIALSKQYFHLCVKLMKAGAHTNISSPSKFLKNSDANSILERPFKFKNDLKKELDNNPLIAMAQINDLYVQIKNNRIRTPTGYAPKEGVSFFKGKSNDAKAHDEVLSVLKELYDSKLTEMLGNLPGEGLEEIKRSQKFFDGELKLLIKNQDISRKVDKKSIQEAVGTSLKLKW
Protein: Cytochrome P450 4F3 (EC 1.14.14.1) (20-hydroxyeicosatetraenoic acid synthase) (20-HETE synthase) (CYPIVF3) (Cytochrome P450-LTB-omega) (Docosahexaenoic acid omega-hydroxylase CYP4F3) (EC 1.14.14.79) (Leukotriene-B(4) 20-monooxygenase 2) (Leukotriene-B(4) omega-hydroxylase 2) (EC 1.14.14.94) (Q08477)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and their oxygenated derivatives (oxylipins). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). May play a role in inactivation of pro-inflammatory and anti-inflammatory oxylipins during the resolution of inflammation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:10409674}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000305|PubMed:10409674}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 4F2
- Cytochrome P450 2J2))
- Cytochrome P450 2C9
- NADPH--cytochrome P450 reductase
- Cytochrome P450 2C19
- Cytochrome P450 2B6
- Prostaglandin G/H synthase 2
- Cytochrome P450 2C8
- Cytochrome P450 2E1
- Cytochrome P450 2U1
Sequence:
MPQLSLSSLGLWPMAASPWLLLLLVGASWLLARILAWTYTFYDNCCRLRCFPQPPKRNWFLGHLGLIHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYIKPVLFAPAAIVPKDKVFYSFLKPWLGDGLLLSAGEKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSARLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVTKRHQQILLYIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCIKESLRLHPPVPAVSRCCTQDIVLPDGRVIPKGIICLISVFGTHHNPAVWPDPEVYDPFRFDPKNIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLGLTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS
Protein: Immunoglobulin heavy variable 3-23 (Ig heavy chain V-III region LAY) (Ig heavy chain V-III region POM) (Ig heavy chain V-III region TEI) (Ig heavy chain V-III region TIL) (Ig heavy chain V-III region TUR) (Ig heavy chain V-III region VH26) (Ig heavy chain V-III region WAS) (Ig heavy chain V-III region ZAP) (P01764)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MEFGLSWLFLVAILKGVQCEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSAISGSGGSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAK
Protein: FhuC protein (Q8Y5U5)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
Interaction partners:
- FhuB protein
- FhuG protein
- Lmo2430 protein
- Probable heme-iron transport system permease protein IsdF
- Lmo1959 protein
- Lmo0541 protein
- Lmo2431 protein
- Lmo1073 protein
- High-affinity heme uptake system protein IsdE
- Cobyric acid synthase
Sequence:
MKDLHTDNLQISYDKRIIVDGLDIAIPANKITALVGANGSGKSTILKTMSRLMKPSKGAVYLDGKTIHSQPTRDVAKQLAILPQNPSAPDGLTVFELISYGRSPHQSSFKSITAKDREIIFWSLRVTNLTEFADRPIDSLSGGQRQRAWIAMALAQETDVLFLDEPTTFLDMTHQLDVLNLLKQLNQSENRTIVMVVHDLNHASRYAHHMIAIKEGKVIAEGTPTSVMTEQTLEDVFNIKADILIDPRSGVPLCLPYETCNGCEIVKELDSIAK
Protein: Pregnancy specific glycoprotein 19 (Psg19 protein) (Q4V8L4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEVSSVLLCSGCSPWQGFLLTASLLTCWLLPTTAQVTLKSSPPQVVEGENVLLSADNLPENIIAFAWYKGETDMNRGIALYSLRYTVSLTGPVHSGRETLYSDGSLWIKNVTQEDTGFYTFRIINNHGKIQSNTTLFLHVKSSLFVCGRPSNIDEPTIESVPVSVSEWGSVLLRVHNLPENLRTLFWYKGVLVLKKLEIARYRTTKNTYELGPVHSGRETVYSNGSLLLQNVTWKDTGFYTLRTLSTDLKVEITHIYLQVNKPVTQPFLRVTVSTVTVQSSVVFTCLSDNTGVSIRWLFKNRNLQVTERMTLSPSNCQLRIHVVRREDAGQYRCEAFNPISSKTSRPVSLAVISE
Protein: Beta-1,4-galactosyltransferase 5 (Beta-1,4-GalTase 5) (Beta4Gal-T5) (b4Gal-T5) (EC 2.4.1.-) (Beta-1,4-GalT II) (Glucosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.274) (Lactosylceramide synthase) (LacCer synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 5) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 5) (Q3YL68)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (By similarity). Required for proper patterning of the dorsoventral axis during embryogenesis through the regulation of BMP signaling. Plays a role in proteoglycan glycosylation that is required for BMP-dependent specification of the dorsoventral axis.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000250|UniProtKB:A0A1S6M251}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
Interaction partners:
- Si:ch73-18b11.1.
- UDP-glucose ceramide glucosyltransferase.
Sequence:
MPTHLRFRRRSFLGLLFLFSLSTSALYFIYSAPGIVNEYLFMVQARGIQIRENVRNMGAQVLEQVVRSAYSINGTDYTYEFNFSETDASPTPFLPEGFTYKPEQVCPEKLPSMKGRLKVNMSEIALDEVEKLLKLNDPGLSVGGHWKPHDCRPRWKVAILVPFRNRHEHLPILFRHLIPALQRQRLQFGFYVIEQAGNEPFNRAMLFNVGFKEAMKDLNWDCVIFHDVDHILENDRNYYGCGEMPRHFAVKLNKYSYMLPYEEFFGGVSGLTVKQFKRINGFPNAFWGWGGEDDDLWNRVQFAGYKVSRPHGELGRYMSIPHHHRGEVQFLGRYKLLRRSKERQSLDGLNNLNYSPLVSRRSLYTNVSVTLSRDLAPVADY
Protein: Phosphodiesterase (EC 3.1.4.-) (Q2V4U0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLSLLCLYFNIHPISVIIFLLTVQAHAVFISLPTDQPDVHLVVLLLAVLMPIFSIKRNEDGMNGVARRKQFKLRPWQSTALPSRHDHYSCAGSATAADGLGGAHLTPSLSSSVHARRESFLYRASDDLREASSLRPVSRASSIASNEHGHGDDLIVTPFAQLLASLRNVRSNLISITNIQNSDDSRHANRSAKRPPLHNIELPDDVVHCAHDTLEELDWCLDQLETIQTHRSVSEMASSKFRKMLNKELSHFAESSKSGTQVSKFLITTYMDKEEDEPSIEIEVPTEVQGPSTSGPMTLSILKKAQTAAMNKISGVRKLRAPSHDGHVPEYGVNCAREIAVHMQRLDDWGPDVFKIDELSKNHSLTVVTFSLLRQRNLFKTFEIHQSTLVTYLLNLEHHYRNNHYHNFIHAADVAQSMHVLLMSPVLTEVFTDLEVLAAIFAGAVHDVDHPGFTNQYLINSNNELAIMYNDESVLEQHHLAVAFKLLQDSNCDFLANLSRKQRLQFRKIVIDMVLATDMSKHMSLLADLKTMVEAKKVAGNNVIVLDKYNDKIQVLQSMIHLADLSNPTKPIELYQQWNQRIMEEYWRQGDKEKELGLEISPMCDRGNVTIEKSQVGFIDYIVHPLYETWADLVYPDAQNILDQLEENREWYQSRIPEEPDTARTVTEDDEHK
Protein: Probable transcription factor At1g66420 (Storekeeper-like protein At1g66420) (Q9C517)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSKKHLKPLETCFEDEEDDVIYLPPGLVTGATSKKNEEFCGGSGKVQPSEMKRRSEGTSTDMTSKRAKKVSAEDEKKVGEWTKNPYFQRLWSEEDEIVMLQGIIKFEDVTGKSPFEDRHGFIEFVKNSISFEASVQQYIGKISQLKRKYTRKRKNGFSEGHEQKCFKLAMSIWGTKETSKKTDLCSSPKGKKVKEEDGDVTNSDWFENSFLLPSIESLGVDSVKRKWNVVPMEFKKKIEERLELLEADESECKKMEEMLKVKNSECVKQKTNLLNEVIDVMT
Protein: T. brucei spp.-specific protein (Q38A03)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWRPAEVNANIGTPPHKVSSIPGLDAGLAPLCATMWAGGLCPTRDVTLWGFGDGDGVGGEQQLRNVQQHSGPSPCAVKEGDEVLMYARPLPSTANEEEDEDGAVRFAQWCTPIERKHASDAGDSSQCSMTGHKARAALAMKRHHGDPGAPTKLPESRACIFSDADELTVPFAKRYRSFQLQGVDDGDSNKVNGSSVLTPCDSSNLSHITPLDEGGESIDLANHMSGLILAASPTPKKLDFVTPLEDGEVHTGDNGTFNAQDGENRPLSACSSTHRPLRGKRFLDDLDPNVGVATSHLSTCKSIREGCRKCRRVDAPEGCGEEKRQRTTDSVRM
Protein: Ubiquitin-conjugating enzyme E2 variant 2 (Q6PEH5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Has no ubiquitin ligase activity on its own. The ube2v2/ube2n heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage (By similarity).
Interaction partners:
- Ube2n protein
- Ubiquitin-conjugating enzyme E2N-like
- Helicase-like transcription factor.
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
- Si:ch211-202a12.4.
- Polyubiquitin-B
- REV3-like, DNA directed polymerase zeta catalytic subunit.
- E3 ubiquitin-protein ligase rnf8
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MAASSGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPARTNYENRIYSLKVECGPKYPEVPPTVRFVTKISMNGINNSNGMVDARSIPILAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYSN
Protein: Phospholipid/glycerol acyltransferase domain-containing protein (G5EE59)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLLSIFYFYGSCITLTYFSTVVLIFFGLSWGVLPQWYLHVVAMIQGYFPREKLENTYENEESEEQRSEKSADQIAEERVKRIIDTDLGPCFQTAPTIRPTLLGMMPEKNWNSTEKAIFFAGLIFRIFFLMPVRVCLLLTSFVFVALAGLQTAFRTLSDREKTWVAIVYCRLFCGSMGLVANYRNPQFRPKKPGVAVSNHLTPNDIQILWAGTPHGSSYGYVVTGQKHKGIIGIIEHLVEKLCPSLWLERKCSNERQGFLAEVMKIAKREGPVLLFPEGYCSNNSKVLQFRKAIFEENVNIYPVAIKQSPEFGDGFWYEDEFFQYLVRIMLNWAVVYDIQYLPMEVRKEHENNSLFAARIQQVIANAAGIPSCEYGGSLWYKQEERNKLKETLKTQHDISGSRNNSDSGISGGGGSSDNLSIDDFESVSENQCEENVIPAMN
Protein: Solute carrier family 12 member 4 (Electroneutral potassium-chloride cotransporter 1) (Erythroid K-Cl cotransporter 1) (mKCC1) (Q9JIS8)
Organism: Mus musculus (Mouse)
Function: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells. May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (Probable).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q28677}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- STE20/SPS1-related proline-alanine-rich protein kinase
Sequence:
MPHFTVVPVDGPRRGDYDNLEGLSWVDYGERAEREDSDGQGNHRENSPFLCPLDASRGNDYYDRNLALFEEELDIRPKVSSLLGKLVSYTNLTQGAKEHEEAESGEGGRRRAAKAPSMGTLMGVYLPCLQNIFGVILFLRLTWMVGTAGVLQALLIVLICCCCTLLTAISMSAIATNGVVPAGGSYFMISRSLGPEFGGAVGLCFYLGTTFAAAMYILGAIEILLTYIAPPAAIFYPSGTHDMSSATLNNMRVYGTIFLTLMTLVVFVGVKYVNKFASLFLACVIISILSIYAGGIKSIFDPPVFPVCMLGNRTLSRDQFDICAKTVVVDNETVATRLWTFFCHSPNLTADSCDPYFLLNNVTEIPGIPGAAAGVLQENLWSAYLEKGEVVEKHGLPSTDTLGLKESLSLYVVADIATSFTVLVGIFFPSVTGIMAGSNRSGDLRDAQKSIPVGTILAIVTTSLVYFSSVILFGACIEGVVLRDKYGDGVSRNLVVGTLAWPSPWVIVVGSFFSTCGAGLQSLTGAPRLLQAIAKDNIIPFLRVFGHGKANGEPTWALLLTALIAELGILIASLDMVAPILSMFFLMCYLFVNLACAVQTLLRTPNWRPRFKYYHWTLSFLGMSLCLALMFVSSWYYALVAMLIAGMIYKYIEYQGAEKEWGDGIRGLSLSAARYALLRLEEGPPHTKNWRPQLLVLLKLDEDLHVKYPRLLTFASQLKAGKGLTIVGSVIQGSFLESYGEAQAAEQTIKNMMDIEKVKGFCQVVVASKVREGLAHLIQSCGLGGMRHNSVVLGWPYGWRQSEDPRAWKTFIDTVRCTTAAHLALLVPKNIAFYPSNHERYLDGHIDVWWIVHDGGMLMLLPFLLRQHKVWKKCRMRIFTVAQMDDNSIQMKKDLAIFLYHLRLEAEVEVVEMHNSDISAYTYERTLMMEQRSQMLRQMRLTKTERDREAQLVKDRHSALRLESLYSDEEEESVAGADKIQMTWTRDKYMAEPWDPSHAPDNFRELVHIKPDQSNVRRMHTAVKLNEVIVTRSHDARLVLLNMPGPPKNSEGDENYMEFLEVLTEGLERVLLVRGGGREVITIYS
Protein: IP06556p (Q9W1S6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO12017p1
- Uncharacterized protein
- GEO02514p1
- LP01981p
- Sex-regulated protein janus-B
- Male-specific transcript 84B, isoform B
Sequence:
MGRKGHKTRRKVKVHSKVHPPQKIKAKLPKRDKRSTLRPKINNSKVFHVNCCKYKIRSRPMRRNQCNLATQCPSHTVAIAPSVPLLHHPVRRKVVHMPETVVMHMRNMEDARRVAVKHRRTLIQTHVPSPDVDDDEDTHQIDRRSRQAYRMGQMRPLSSDVDVDDMDVDPFQ
Protein: Multifunctional methyltransferase subunit TRM112-like protein (tRNA methyltransferase 112 homolog) (Q9DCG9)
Organism: Mus musculus (Mouse)
Function: Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA (By similarity). The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor. The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species (By similarity). Together with methyltransferase THUMPD3, catalyzes the formation of N(2)-methylguanosine at position 6 in a broad range of tRNA substrates and at position 7 of tRNA(Trp) (By similarity). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production (By similarity). Together with methyltransferase METTL5, specifically methylates the 6th position of adenine in position 1832 of 18S rRNA (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UI30}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UI30}. Note=Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes. {ECO:0000250|UniProtKB:Q9UI30}.
Interaction partners:
- rRNA N
- Methyltransferase HEMK2
- 18S rRNA
- tRNA wybutosine-synthesizing protein 2 homolog
- tRNA
- Probable tRNA methyltransferase 9B
- Methyltransferase like 27
- Ubiquitin-like protein FUBI
- rRNA N
- MTRF1L release factor glutamine methyltransferase
Sequence:
MKLLTHNLLSSHVRGVGTRGFPLRLQATEVRINPVEFNPEFVARMIPKVEWAALVQAADTLNLAEVPKEPTEGYEHDETFLRKMHHVLLEVDVLEGTLQCPESGRLFPISRGIPNMLLNDEETET
Protein: F-box domain-containing protein (Q59WC4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MNSLTDLPIDLLQRIIEETNRLDNHKNPSYSSLFSLSQTCRFFNRLINQVLYQHITIYDNDNKSIIQTTNQTYIHIDHLSKFIEGLSMSNFQYIKSIHIHCKSNFSSFNYDSLYTKLNQYWSYLNHPIEFINFDVENIRQKQSLDQFLSNNNCTNIMEENDEVGGVCDIHSSVSKLCNLSNLSILKVQELNQIPCHNPNLKNLNLFIEGNFMDEYIKDRVLNLEQLEILQLNTTLSTKVFVNSNINCPNLEKLSICYCHSLRESPLTFSQFAAIDFGKLIELELKLNCFHRDCDCINQFYNDLTKAQHANEFNNLQKLSIINYKSKNSSNNLCQYNYVINCQLESIFRKFPKLDYLYFNLNEFTKNDQFKINWAKFAESLQILKNLKTLIIYDFFNYWLPSMKSNQATSEILLNNCKCVECNQRRSAFNSMAEYDAANNYVHNFKNYTEPELSAESGNEYQPILLNKKCNAKLLWFIFSQLQSQQFKQSPIYSMNLSYFREDKELFSQFQELFKHNCLNNLCNDIKIGNNNTKTINLGGIVN
Protein: RIKEN cDNA 2310061I04 gene (B8JJ67)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVLPPRKREKGPGPELHSGCLDGLRSLFEGPPCPYPGAVIPFQAPGPSHSSPTTPSGDESMEEHLAVMHERLRQELPTLFLRSHDYTIYSMDVEFINEILNIRTKGRTFYVMSLTLCRFLVWNYFAQFRL
Protein: Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC 1.2.4.1) (PDHE1-A type I) (P35486)
Organism: Mus musculus (Mouse)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:19341700}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Pyruvate carboxylase, mitochondrial
- L-lactate dehydrogenase A chain
- Pyruvate kinase PKM
- [Pyruvate dehydrogenase
- L-lactate dehydrogenase B chain
Sequence:
MRKMLAAVSRVLAGSAQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLPVRAILAELTGRRGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATKFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS
Protein: Carbonyl reductase [NADPH] 1 (EC 1.1.1.184) (15-hydroxyprostaglandin dehydrogenase [NADP(+)]) (EC 1.1.1.196, EC 1.1.1.197) (20-beta-hydroxysteroid dehydrogenase) (Alcohol dehydrogenase [NAD(P)+] CBR1) (EC 1.1.1.71) (NADPH-dependent carbonyl reductase 1) (Prostaglandin 9-ketoreductase) (PG-9-KR) (Prostaglandin-E(2) 9-reductase) (EC 1.1.1.189) (P48758)
Organism: Mus musculus (Mouse)
Function: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol (By similarity). Can convert prostaglandin E to prostaglandin F2-alpha (By similarity). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q28960}.
Interaction partners:
- Carbonyl reductase 2
- Carbonyl reductase 3
- Prostaglandin E synthase 2
- Prostaglandin E synthase 3
- Prostaglandin E synthase
- UDP-glucuronosyltransferase 1A6
- Cytochrome P450 1A1
- Dihydrofolate reductase
- Sepiapterin reductase
- Cytochrome P450 2E1
Sequence:
MSSSRPVALVTGANKGIGFAITRDLCRKFSGDVVLAARDEERGQTAVQKLQAEGLSPRFHQLDIDNPQSIRALRDFLLKEYGGLDVLVNNAGIAFKVNDDTPFHIQAEVTMKTNFFGTRDVCKELLPLIKPQGRVVNVSSMVSLRALKNCRLELQQKFRSETITEEELVGLMNKFVEDTKKGVHAEEGWPNSAYGVTKIGVTVLSRILARKLNEQRRGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVQDKKVEPW
Protein: Palmitoyltransferase ZDHHC20 (EC 2.3.1.225) (Acyltransferase ZDHHC20) (EC 2.3.1.-) (DHHC domain-containing cysteine-rich protein 20) (DHHC20) (Zinc finger DHHC domain-containing protein 20) (Q5W0Z9)
Organism: Homo sapiens (Human)
Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation. Has a preference for acyl-CoA with C16 fatty acid chains. Can also utilize acyl-CoA with C14 and C18 fatty acid chains.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:29326245}; Multi-pass membrane protein {ECO:0000269|PubMed:29326245}. Cell membrane {ECO:0000269|PubMed:27153536}; Multi-pass membrane protein {ECO:0000269|PubMed:29326245}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAPWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVELCVFTIFGNEENGKTVVYLVAFHLFFVMFVWSYWMTIFTSPASPSKEFYLSNSEKERYEKEFSQERQQEILRRAARALPIYTTSASKTIRYCEKCQLIKPDRAHHCSACDSCILKMDHHCPWVNNCVGFSNYKFFLLFLLYSLLYCLFVAATVLEYFIKFWTNELTDTRAKFHVLFLFFVSAMFFISVLSLFSYHCWLVGKNRTTIESFRAPTFSYGPDGNGFSLGCSKNWRQVFGDEKKYWLLPIFSSLGDGCSFPTRLVGMDPEQASVTNQNEYARSSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN
Protein: Uracil-DNA degrading factor, isoform B (Uracil-DNA degrading factor, isoform C) (Uracil-DNA degrading factor, isoform D) (Q7KS11)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAEGDSKFGFKDMEKALETLKLLESHDMQYRKLTVRGLLGRAKRVLTMTKAEEKLKNINAAIGVFEKWLEENGGGASSKNAKTESEDKVETVPGLGFKDKAAAEATLSILAERDPDYQRLAIKGLIGSSKRVLSGTKNEDKITAIKEGVQVLEDFLEKFEAENRIKDNRAYLPLAVVTKLPDPKDELAKEFLEAYGGSKAKGNYKHLRTMFPKTDEKTSWDIVRNRQLSKLLEQIKSEEAKLFDAETGAPTDLHLQLIHWAYSPQPDKLKQYIEKLAKKTPEKRKQESSSSASDSSATSQDSDGEDKPKRKKKREE
Protein: Nucleic acid-binding, OB-fold-like protein (Putative replication protein; 94555-97079) (Q9C926)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Zinc knuckle
- Uncharacterized protein
- Phosphatidylinositol 3-and 4-kinase family protein
- Ankyrin repeat family protein
- Putative cysteine-rich repeat secretory protein 24
- Replication protein A 32 kDa subunit A
- Replication protein A 32 kDa subunit B
- Sister chromatid cohesion protein PDS5 homolog E
- DNA mismatch repair protein MSH2
- Protein disulfide-isomerase 5-4
Sequence:
MDEVNPYTAIKNLKPFKTSWCIQVKILHAWNHYTKGSGMSYEMMLADEDGNKIQAGIKKEHLLKLQRYVKIGHWTIIEEFSVTKASGLYRSTTHPYRINIQSSTRFSNSPTISDEIWLDLVNFNDVLSGTLDQNKLVNVIGQLVNVGEIQLLDVQGKPTKKIDFQLRDTDDNRLPCSLWGKFADQIHKVSKESVGGIVICLIRWAKLGHYKEIRSISNAFDASEVFINPILTEVEEFKNLLPSDGLALTIMEPKPRFQPLRVREERSKQFERKTIAELKASFEVEKVKIICSILSIDLDYSWYYYAHIKCNKKVFKSKKTLSSGAKKIIYRCDKCATDVTSIEARYWLHLDIMDNTGESKLMLFDSFVEPIIGCPATELLDVTNEQIDEPQPLPDVVKNIIGKTYQFLVCVEQDNISRGNDEYKVAEVLTSQNINQALPINDSVNPVDHSSISSNDQVLMLTNNSEKEDNSQTLSRTPLSKRKEIVDDGSDQSSTSKKQCTKDSDETVTDVTVIDVDNPNDWHEPKFFHKLEEAAQGNLKEVKHEREKIVLKNIKVEKIDGKNAPK