wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (GNT-I) (GlcNAc-T I) (EC 2.4.1.101) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I) (P70680)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU368119}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU368119}.
Interaction partners:
Sequence:
MLKKQSAGLVLWGAILFVGWNALLLLFFWTRPAPGRPPSDSAIDDDPASLTREVFRLAEDAEVELERQRGLLQQIREHHALWRQRWKVPTVAPPAWPRVPATPSPAVIPILVIACDRSTVRRCLDKLLHYRPSAEHFPIIVSQDCGHEETAQVIASYGSAVTHIRQPDLSNIAVPPDHRKFQGYYKIARHYRWALGQIFNKFKFPAAVVVEDDLEVAPDFFEYFQATYPLLRTDPSLWCVSAWNDNGKEQMVDSSKPELLYRTDFFPGLGWLLMAELWTELEPKWPKAFWDDWMRRPEQRKGRACIRPEISRTMTFGRKGVSHGQFFDQHLKFIKLNQQFVSFTQLDLSYLQREAYDRDFLARVYSAPLLQVEKVRTNDQKELGEVRVQYTSRDSFKAFAKALGVMDDLKSGVPRAGYRGVVTFQFRGRRVHLAPPQTWEGYDPSWT
Protein: ERCC4 domain-containing protein (P95024)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- DNA polymerase I
- DNA topoisomerase 1
- Putative lipoprotein LprE
- 5'-3' exonuclease
- Protein RecA
- Large ribosomal subunit protein uL1
- Probable helicase HelZ
- Uncharacterized protein
- Putative lipoprotein LppK
- Beta sliding clamp
Sequence:
MHLAHRVASSRDTPSSSATPNAVSGSASNAADRPCLVRPPTAPPWAHGPRLRRDPTGGGSTPSIVLSRSTDRSKDGHRIVPAGARKSGVRASTGRLPSTRKTTRSPDCRPSASRTAFGTVTCPFDVTMGSSECLLHRCRTPPVPSHSVELLVAANPAEDSRLPYLIRLPVGAGLVFATSDVWPRTKALYCHRLDIADWPADPVVVDRVELRSCSRRGAAIDVVAARARENRSQLVHTMARGRQVVFWQSPKTRKQSRPGVRTPTARAAGIPELHIVVDAHERYPYTFADKPAKTTREALPCGDYGLKVAGQLVAAVERKALADLTSGVLNGNLKYQLTELAALPRAAVVVEDRYSEIFAHSFARPTAIADGLAELQIGFPNVPIVFCQTRKLAQEYTYRYLAAALTWFVDDADATTVFEPAAAEPEPSSAELRAWAKSVGLPVSDRGRLRPQILQAWRAAHPR
Protein: Decaprenyl diphosphate synthase (DecaPP) (EC 2.5.1.86) (EC 2.5.1.87) (Decaprenyl pyrophosphate synthase) (Long-chain isoprenyl diphosphate synthase) (Trans,polycis-decaprenyl diphosphate synthase) (P9WFF7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) in the cis configuration with (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP) generating the 50 carbon product trans,polycis-decaprenyl diphosphate. When (2E,6E)-farnesyl diphosphate (E-FPP or EE-FPP) is used in vitro, both primary products decaprenyl diphosphate and (2E,6E,10E)-geranylgeranyl diphosphate (EEE-GGPP) are synthesized. M.tuberculosis does not synthesize (2E,6E,10Z)-geranylgeranyl diphosphate (EEZ-GGPP) and heptaprenyl diphosphate. Can also accept many different allylic substrates, including E-geranyl diphosphate (E-GPP), neryl diphosphate (NPP), and all-trans-geranyl-geranyl diphosphate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10816587, ECO:0000269|PubMed:11004176}.
Interaction partners:
- 
- Uncharacterized protein
- Nonaprenyl diphosphate synthase
- DNA repair protein RecO
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 
- 
- Phosphatidate cytidylyltransferase
- Putative amidase AmiA2
- Geranylgeranyl diphosphate synthase
Sequence:
MARDARKRTSSNFPQLPPAPDDYPTFPDTSTWPVVFPELPAAPYGGPCRPPQHTSKAAAPRIPADRLPNHVAIVMDGNGRWATQRGLARTEGHKMGEAVVIDIACGAIELGIKWLSLYAFSTENWKRSPEEVRFLMGFNRDVVRRRRDTLKKLGVRIRWVGSRPRLWRSVINELAVAEEMTKSNDVITINYCVNYGGRTEITEATREIAREVAAGRLNPERITESTIARHLQRPDIPDVDLFLRTSGEQRSSNFMLWQAAYAEYIFQDKLWPDYDRRDLWAACEEYASRTRRFGSA
Protein: Berberine bridge enzyme-like 6 (AtBBE-like 6) (EC 1.1.1.-) (Flavin-dependent oxidoreductase FOX4) (EC 1.-.-.-) (Q9FZC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable flavin-dependent oxidoreductase.
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:O64743}.
Interaction partners:
- Endoglucanase 4
- Peroxidase 37
- AT1G22750 protein
- Peroxidase 38
- Receptor-like protein 53
- Isopentenyl phosphate kinase
- Receptor-like protein 43
- Insecticidal crystal toxin domain-containing protein
- Thioredoxin H7
- Thioredoxin H8
Sequence:
MKEAFVFLLCLTNKFPKKFNSCSKKKETLYVLGLVLLVSFIEAPVTKPNFGKFIECLRDRTTPENPITDVISIADNSTTFLSSYVSYTKNKRFSSPNFKKLLAIIAAKHVSHVQATVVCAKSNGIQLRIRSGGHDNEGFSYMSSVPFVILDMHNLRSIDVNLSRKNAWVQAGATLGELYVKINEASQTLAFPAGVCPTVGAGGHISGGGFGNLMRKFGITVDHVIDAQIIDVNGKLLNRAAMGEDLFWAIRGGGSSFGVILSWKINLVEVPKILTVFKVNKTLEQGGTDILYKWQLVANKLPDSLFITAWPRTVNGPKPGERTVAVVFYAQFLGPTDKLMEIMDQSFPELGLGREDCHEMSWLNTTLFWANYPAGTPKSILLDRPPTNSVSFKSKSDFVKKPIPKKGLEKLWKTMFKFNSSVSLQFNPYGGVMDRIPATATAFPHRKGNLFKVQYSTMWFDANATESSLAMMNELFEVAEPYVSSNPREAFFNFRDIDIGSNPSGETNVDEAKIYGSKYFLGNLKRLMDVKAKYDPDNFFKNEQSIPPVRVK
Protein: Rho GTPase-activating protein 42 (Rho GTPase-activating protein 10-like) (Rho-type GTPase-activating protein 42) (A6NI28)
Organism: Homo sapiens (Human)
Function: May influence blood pressure by functioning as a GTPase-activating protein for RHOA in vascular smooth muscle.
Interaction partners:
- Putative keratin-associated protein 20-4
Sequence:
MGLPTLEFSDSYLDSPDFRERLQCHEIELERTNKFIKELIKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVEEERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILEKHLNLSAKKKESHLQEADTQIDREHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYKQQLQFNLQNTRNNFESTRQEVERLMQRMKSANQDYRPPSQWTMEGYLYVQEKRPLGFTWIKHYCTYDKGSKTFTMSVSEMKSSGKMNGLVTSSPEMFKLKSCIRRKTDSIDKRFCFDIEVVERHGIITLQAFSEANRKLWLEAMDGKEPIYTLPAIISKKEEMYLNEAGFNFVRKCIQAVETRGITILGLYRIGGVNSKVQKLMNTTFSPKSPPDIDIDIELWDNKTITSGLKNYLRCLAEPLMTYKLHKDFIIAVKSDDQNYRVEAVHALVHKLPEKNREMLDILIKHLVKVSLHSQQNLMTVSNLGVIFGPTLMRAQEETVAAMMNIKFQNIVVEILIEHYEKIFHTAPDPSIPLPQPQSRSGSRRTRAICLSTGSRKPRGRYTPCLAEPDSDSYSSSPDSTPMGSIESLSSHSSEQNSTTKSASCQPREKSGGIPWIATPSSSNGQKSLGLWTTSPESSSREDATKTDAESDCQSVASVTSPGDVSPPIDLVKKEPYGLSGLKRASASSLRSISAAEGNKSYSGSIQSLTSVGSKETPKASPNPDLPPKMCRRLRLDTASSNGYQRPGSVVAAKAQLFENVGSPKPVSSGRQAKAMYSCKAEHSHELSFPQGAIFSNVYPSVEPGWLKATYEGKTGLVPENYVVFL
Protein: Carbon disulfide hydrolase (CS(2) hydrolase) (EC 3.13.1.5) (Carbon disulfide lyase) (G0WXL9)
Organism: Acidianus sp. (strain A1-3)
Function: Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism that allows Acidianus sp. A1-3 to grow on carbon disulfide as the main carbon and energy source. Does not show carbonic anhydrase activity (hydration of CO(2) to carbonate).
Interaction partners:
Sequence:
MVSEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHIEQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKEIIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLPAFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHPLIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIVKE
Protein: Protein OCA4 (Oxidant-induced cell-cycle arrest protein 4) (P25366)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for replication of Brome mosaic virus (BMV).
Interaction partners:
- Tyrosine-protein phosphatase-like protein OCA2
- Inositol diphosphatase SIW14
- Putative tyrosine-protein phosphatase OCA1
- Oxidant-induced cell-cycle arrest protein 5
- Putative uncharacterized protein YCL042W
- Uncharacterized protein YCR024C-B
- Putative tyrosine-protein phosphatase OCA6
- GTP-binding protein YPT1
Sequence:
MLVPPANFGIAEEGIYRCSKVETLNLSFLETLNLKTAIFIGGQEPSKFFKDFFTRSSIKWIVLRMSDFSAAAVPVKSSSVSNANLYSNNNSTLSLQEEKKKSTANGSQNSTTGDPVIQEELAYHLTDNDDLMLIKSTCLKRTFKTLLNVDNYNVLLVDKTALVIGILRKIQKWNIASIINEYRLFSGKNRNYFAETFLEIINIEIEQEKDNKTIVDNKAKKLPLENNRTHSIEYKANSGKLIRVNEDDLCREPEVPQRLLTLINQIETKVKNNKVLQVSGVLGDDLKKTSSDLGIFGHRYRLAFNKKENGDYGYYKARGKDNVKIRIPCDSELPDWFRFQRDLWEKENVPEEHHFYREHIFT
Protein: Aldo-keto reductase family 1, member B8 (Q6AY99)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Sorbitol dehydrogenase
- Aldehyde dehydrogenase family 3 member A2
- Carbonyl reductase 1])
- Carbonyl reductase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase, mitochondrial
- 4-trimethylaminobutyraldehyde dehydrogenase
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- L-xylulose reductase
Sequence:
MAAFVKLSTKAKMPIVGLGTWKSPPDKVKEAVKAAIDAGYRHFDCAYVYQNESEVGEAIQEKIKEKAVRREDLFIVSKLWPTFFEKSLVKKAFQKTLLDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGNVLTSKYTFLDAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPSAKPEDPVLLEIPKIKEIASKHKKTAAQVLIRFHIERNVAVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRACGLFAASRNEDFPFHSEY
Protein: Cyclin-C (Q86KE7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Binds to and activates cyclin-dependent kinase CDK8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Probable cyclin-dependent kinase 8
- Putative mediator of RNA polymerase II transcription subunit 18
- Putative mediator of RNA polymerase II transcription subunit 14
- Putative mediator of RNA polymerase II transcription subunit 6
- Putative mediator of RNA polymerase II transcription subunit 7
- Putative mediator of RNA polymerase II transcription subunit 10
- Putative mediator of RNA polymerase II transcription subunit 12
- Putative mediator of RNA polymerase II transcription subunit 21
- Putative mediator of RNA polymerase II transcription subunit 31
- Putative mediator of RNA polymerase II transcription subunit 27
Sequence:
MAANFWESSHCTEWLLDRNKIEESNPKDKQYLTPIELKKLRTHYCFVIQNLGNALKLRQRAISTAIVYFKRFYLKNSFVDCEPRLVAVTCLYLSSKVEECITQAKKCAAKMKEIDHSFNYLMNDILECEFFVLEELDFCLIIYHPYKSLPFYLQSSGLDPASIEIIWGIVNDSYRTDVCLLYPPFVVGLGCILLGSYLLKKDIKQWLSELNVEMKDIWEVSKDLIDYYEFEKQQSLQNQSELDLLYNKLPIRNKK
Protein: 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) (C1BI43)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MAFFTHQVIRGLSSSAVRNAAIKHVTIIGGGQMGAGIAQVAATTGHSVVLVDTNEEILKKSAKGIEGSLKRVVKKKFADKPDAGAEFIAKVMANVSISTDAASVVGSTDLVLEAIVENLKIKQGLFGALDKVAPAHTIFASNTSSLPITDIASSTSRLDRFGGLHFFNPVPMMKLVEVIGTSATSQDTFDSLLAFSKALGKTPVSCKDTPGFIVNRLLVPYMMEAIRLHERGHGSKEDIDIAMKLGAGYPMGPFELLDYVGLDTAKFIMDGWVEKDPDNPLMQPSEMLNKLVAEGKFGKKTGEGFYKYK
Protein: Alpha-(1,3)-fucosyltransferase 7 (EC 2.4.1.-) (Fucosyltransferase 7) (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase) (Q11131)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization. In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors (By similarity). However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc (By similarity). Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation. May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium (By similarity). May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi.
Interaction partners:
- Type 2 lactosamine alpha-2,3-sialyltransferase
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Alpha-
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- P-selectin
- E-selectin
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Galactoside alpha-
- Alpha-
- P-selectin glycoprotein ligand 1
Sequence:
MPTPCPPACLSTPGTHRLLPFPDWKAPSWESRKEATCNSSSPGPWAEPTVQGYHPTRRLRAWGGLAGGATFMVIWFFWLWGSAPGSAPVPQSTLTILIWHWPFTNRPPELPGDTCTRYGMASCRLSANRSLLASADAVVFHHRELQTRQSLLPLDQRPHGQPWVWASMESPSNTHGLHRFRGIFNWVLSYRRDSDIFVPYGRLEPLSGPTSPLPAKSRMAAWVISNFQERQQRAKLYRQLAPHLQVDVFGRASGRPLCANCLLPTLARYRFYLAFENSQHRDYITEKFWRNALAAGAVPVALGPPRATYEAFVPPDAFVHVDDFSSARELAVFLVSMNESRYRGFFAWRDRLRVRLLGDWRERFCTICARYPYLPRSQVYEDLESWFQA
Protein: Signal peptidase complex catalytic subunit SEC11 (EC 3.4.21.89) (Signal peptidase complex catalytic subunit sec11) (Q9SSR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648}.
Interaction partners:
- Cyanate hydratase
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3B
- Signal peptidase complex subunit 3A
- Probable galacturonosyltransferase 7
- signal peptidase I
- Probable glutamyl endopeptidase, chloroplastic
- Probable thylakoidal processing peptidase 2, chloroplastic
- Thylakoidal processing peptidase 1, chloroplastic
Sequence:
MGWIGETVDSIKSIQIRQLFTQAISLGMIVTSALIIWKALMCVTGSESPVVVVLSGSMEPGFKRGDILFLHMSKDPIRAGEIVVFNVDGRDIPIVHRVIKVHERENTGEVDVLTKGDNNYGDDRLLYAEGQLWLHRHHIMGRAVGFLPYVGWVTIIMTEKPIIKYILIGALGLLVITSKD
Protein: Beta-1,3-galactosyltransferase pvg3 (EC 2.4.1.134) (Meiotically up-regulated gene 49 protein) (Pyruvylated Gal-beta-1,3-epitope synthesis protein 3) (PvGal synthesis protein 3) (Q9USX0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cell wall biogenesis. Has a role in the addition of Gal-beta1,3 moeities to galactomannans and their subsequent pyruvylation. Has a role in meiosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pyruvyl transferase 1
- Pyruvylated Gal-beta-1,3-epitope synthesis protein 2
- Pyruvylated Gal-beta-1,3-epitope synthesis protein 5
- MADS-box transcription factor pvg4
Sequence:
MFSNSKKKIFLYVLIAGVATFSFAFLVLNRLQAEEHSLAYVENLFLDPFIKQNESLAHANDRPFKLYLGIFSQAKNVDRRNFLRTDYNEYIKEFAVNDTVDVRFILGLPENEQELATIREEQRTYGDLAVLPIPENVDAGKSIVYFQTFLEGYQPFPLFSELADNLIMPSTQFHGSFIYNQSIKTYELPGMKEFQDLGEPKHDYDFIVKADDDSFLNLPRLFEMLKEHVGKSRFYFGRDCTRRELPTAVRDFPYMCGFFYIVSPDMAYEVAKRRNIIIPFEDAQTGYSIYLSGNVKNAEFSKCTLYDLILPNEGFNYRQSYLRIDAIAVHKLKSIPLLSTVSNWFKKMYEHRANCSALIETERLSCLQATIPLPSLDV
Protein: 4.1G isoform (Erythrocyte membrane protein band 4.1 like 2) (Q6R5J7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEEETQLEEELDKAQEDILKHQASISELKRNFMESTPEPRPNEWEKRRITPLSLQTQGSSHETLNIVEEKKRAEVGKDERVITEEMNGKEISPGSGPGEIRKVEPVTQKDSTSLSSESSSSSSESEEEDVGEYRPHHRVTEGTIREEQEYEEEVEEEPRPAAKVVEREEAVPEASPVTQAGASVITVETVIQENVGAQKIPGEKSVHEGALKQDMGEEAEEEPQKVNGEVSHVDIDVLPQIICCSEPPVVKTEMVTISDASQRTEISTKEVPIVQTETKTITYESPQIDGGAGGDSGTLLTAQTITSESVSTTTTTHITKTVKGGISETRIEKRIVITGDGDIDHDQALAQAIREAREQHPDMSVTRVVVHKETELAEEGED
Protein: Mutant ornithine transporter 2 (Solute carrier family 25 (Mitochondrial carrier, Ornithine transporter) member 2) (Q99ML6)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MQTFPQLYKGLADCFLKTYNQVGIRGLYRGTSPALLAYVTQGSVLFMCFGFCQQFVRKVARVEQNAELNDLETATAGSLASAFAALALCPTELVKCRLQTMYEMKMSGKIAQSYNTIWSMVKSIFMKDGPLGFYRGLSTTLAQEIPGYFFYFGGYEISRSFFASGGSKDELGPVPLMLSGGFAGICLWLIIFPVDCIKSRIQVLSMFGKPAGLIETFISVVRNEGISALYSGLKATLIRAIPSNAALFLVYEYSRKMMMNMVEEY
Protein: Thioredoxin/glutathione peroxidase BtuE (EC 1.11.1.24) (EC 1.11.1.9) (P06610)
Organism: Escherichia coli (strain K12)
Function: Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate.
Subcellular location: Periplasm {ECO:0000305|PubMed:3528129}. Note=Appears to have a periplasmic location. It has the mean hydropathy of a soluble protein but lacks an obvious signal sequence. {ECO:0000305|PubMed:3528129}.
Interaction partners:
- Vitamin B12 import ATP-binding protein BtuD
- Glutathione reductase
- Glutathione S-transferase GstA
- Glutathione S-transferase YfcF
- Vitamin B12 import system permease protein BtuC
- Glutathione hydrolase proenzyme
- Glutathione synthetase
- Glutathione S-transferase GstB
- Glutathione-specific gamma-glutamylcyclotransferase
- Bifunctional glutathionylspermidine synthetase/amidase
Sequence:
MQDSILTTVVKDIDGEVTTLEKFAGNVLLIVNVASKCGLTPQYEQLENIQKAWVDRGFMVLGFPCNQFLEQEPGSDEEIKTYCTTTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTAVAPEESGFYARMVSKGRAPLYPDDILWNFEKFLVGRDGKVIQRFSPDMTPEDPIVMESIKLALAK
Protein: bZip transcription factor GAP1 (Q6FRZ8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Transcription factor that plays a critical role in response to various stresses and reduces the stress through transcriptional activation of its target genes including multidrug transporter FLR1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Transcription factor
Sequence:
MAEVDNGGAQKSSASRKKRYQELDPETRMKRVAQNRAAQKAFRERKERKMKELERKVVDLENLTKLNEVETNFLRDQLSILVKELRKYRPETKQDHKVLKYLEKHKGGAAGAGNGAATGSVSTSTRHTDLAASNANRVSKDSSILPGAKIIRQDLESFNENRHFNVTGQLTPPGNTSSSTTANSVAANAKKQSIPHSDSSDSNESKNTWNTDPTSSEDWLDDVMTSHKQISRGQSGSGIDFNNFFDEQVSEFCTKLNQACGTKACPIPQSKSAATTPLPGTSSNGNSNSPMIINDTMGDVSLNMQGNEHGNATNNLVTDPAFLSNTWDDMSPASNQHSTGGAPGFGQLGFGDNLLGNDILFSPNSPAYSPSVLGSGRTQEVYRSPAVQKVVEKENESKSVNFPFINSSLAFPGDYDNNFFRETTDLNFDDNDQDDNFTNSNDLVNDYFTTNIPDTDNSDSALIANGLVKEEPSMQTEDTFKVQNTNDMLNSSRMKETIDNQNIGEKTTKDDNEDDDEDDENDNTVVPSRDDGLLRCSEIWDRITAHPKYSDIDIDGLCSELMAKAKCSERGVVINADDVQVALNKHMS
Protein: Parvalbumin (E0WDA3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MAFAGLNDADVAAALAACTAADSFNHKAFFAKVGLAGKSNDDVKKAFYVIDQDKSGFIEEDELKLFLQNFSASARALTDAETKAFLADGDKDGDGMIGVDEFAAMIKG
Protein: Hippocalcin-like protein 4 (HLP4) (Q9UM19)
Organism: Homo sapiens (Human)
Function: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation.
Interaction partners:
- Protein FAM131C
Sequence:
MGKTNSKLAPEVLEDLVQNTEFSEQELKQWYKGFLKDCPSGILNLEEFQQLYIKFFPYGDASKFAQHAFRTFDKNGDGTIDFREFICALSVTSRGSFEQKLNWAFEMYDLDGDGRITRLEMLEIIEAIYKMVGTVIMMRMNQDGLTPQQRVDKIFKKMDQDKDDQITLEEFKEAAKSDPSIVLLLQCDMQK
Protein: PH domain-containing protein (Q54PT8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKSSNGVGCTDSIQGYLFKKGNSSLLSSSSTLWKKRWFSLENGSTTLKYFKNSSDESPKGSINIQLIESIDILTTTTTTTTTTTTFGNKDNTNNNNNNNNNNNNSKYYFDLKIKSRVYHLYSETERERDYWNVNLNLSILKSKEPSPSLSPQSQVRPRSYTLPSPTPTIVLAEPSPSPSPTPLPPLPIPPNNKTKPPLPPKPISQQQQQPVQQQQHQQQQQQHPTTNTNTNGNSNNNNVILNKKQQQQQQQPVKQKEIENEENFEYEDDDISLCGAKRKDFIKNHSSGYITSMVGVTRSKIWCGDSQGNICTFTLSRNGSGANGITDKVKKGSQWKEHTLMVTSLVYVPSQKLVYSSSLDGKICAWDRTDYSLLFSHSSKFPIYDMLFSKNDLLVYCGGISSSQQQQQQQQQNQNLQNQNQNLSLFDTVTKEETEIPFQSFLPNLYNNGNSGNKKRKFIKMVKFDEKIIICTDRCEIIVWSPWDNEICKYVKINNSYDITAMNVVGENLWICTTSDTNGNIFSTTNPCLVIVLSIKTALKRVKSFECRHPISQFTLVNGYVWAITRDYITVYEQNTAQLAYETIILKEDMNFKLLYNFNTVWVGGTWLFRFQIFNNWIRDNLEYTTNSSSSPDKSAASSSAISINIQPISDYSDFDNVLNVLELIKERLQYDHCNQLYDILLGICENDQLNLTDFKILTSKSFRWFGRNQCSSVMRESIVSDNNRVYRISRVLSNYLQQSNIKDYYINIRESSNNITINGSGSGNGSINSSNGSINNSGGSNSSGYNSNVIFIYETLKTVEYLVSNFDKFSKQFQIQQQFIETIIKFTTLSLPSNRLIVSISLIILYHLLNSNGNNLLNISSSSSSPSSSPNLSINDGLITTTPTSTNNTTTTTTTTTTTTTTNNSSSSVTKKIKENFKVNKNKDKDKESKGNKEINNNSKDNIKENTIKDIGGNSLYNNLKDKVKLYLSVFFDQSIDDKTKISIINVLSRFPTELKEQFKKELYLNSTFQLLNQGISLVCNDLIIIMNQILIDSPKIKDQIIKYVPNLLNLLDQKQQQQPINDRIRIFQIMSNPTFIQRSYNNNSIGNNNNDNKKLKNRKVIISSNFKSPIESILFTINSILHSLKSTSFRGLKITILDIIVPKEFNQDLLSSINGSIINLNFILPNQSFVSTIKFKFNPKDLAIKVAFQLGVSVGETTISNFSITGDLQLGFTLGTAKPEYISFLEDPIINFDFDSTGVINLIDKFVKPILKKSIRKRLVHPNRFYLPSS
Protein: cullin-RING-type E3 NEDD8 transferase (EC 2.3.2.32) (A0A0G2JUC8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAAMDVDTPSGTNSGAGKKRFEWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKKDSPVKLTHLLLV
Protein: Transcription factor EGL1 (Basic helix-loop-helix protein 2) (AtMYC146) (AtbHLH2) (bHLH 2) (Protein ENHANCER OF GLABRA 3) (Transcription factor EN 30) (bHLH transcription factor bHLH002) (Q9CAD0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator, when associated with MYB75/PAP1, MYB90/PAP2 or TT2. Involved in epidermal cell fate specification. Regulates negatively stomata formation but promotes trichome formation. Together with MYB66/WER, promotes the formation of non-hair cells in root epidermis cells in the N position. Whereas together with CPC, promotes the formation of hair cells in root epidermis cells in the H position by inhibiting non-hair cell formation. Seems also to play a role in the activation of anthocyanin biosynthesis, probably together with MYB75/PAP1. Involved in seed mucilage production. Activates the transcription of GL2.
Subcellular location: Nucleus {ECO:0000305}. Note=Moves from developing hair cells (trichoblasts) to developing non-hair cells (atrichoblasts). {ECO:0000250}.
Interaction partners:
- Protein TRANSPARENT TESTA GLABRA 1
- Transcription factor WER
- Transcription factor MYB75
- Transcription factor MYB114
- Transcription factor MYB113
- Transcription factor CPC
- Transcription factor MYB90
- Transcription factor GLABRA 3
- Transcription factor MYB23
- Transcription factor TT2
Sequence:
MATGENRTVPDNLKKQLAVSVRNIQWSYGIFWSVSASQPGVLEWGDGYYNGDIKTRKTIQAAEVKIDQLGLERSEQLRELYESLSLAESSASGSSQVTRRASAAALSPEDLTDTEWYYLVCMSFVFNIGEGIPGGALSNGEPIWLCNAETADSKVFTRSLLAKSASLQTVVCFPFLGGVLEIGTTEHIKEDMNVIQSVKTLFLEAPPYTTISTRSDYQEIFDPLSDDKYTPVFITEAFPTTSTSGFEQEPEDHDSFINDGGASQVQSWQFVGEEISNCIHQSLNSSDCVSQTFVGTTGRLACDPRKSRIQRLGQIQEQSNHVNMDDDVHYQGVISTIFKTTHQLILGPQFQNFDKRSSFTRWKRSSSVKTLGEKSQKMIKKILFEVPLMNKKEELLPDTPEETGNHALSEKKRREKLNERFMTLRSIIPSISKIDKVSILDDTIEYLQDLQKRVQELESCRESADTETRITMMKRKKPDDEEERASANCMNSKRKGSDVNVGEDEPADIGYAGLTDNLRISSLGNEVVIELRCAWREGILLEIMDVISDLNLDSHSVQSSTGDGLLCLTVNCKHKGTKIATTGMIQEALQRVAWIC
Protein: Small ribosomal subunit protein eS28x (40S ribosomal protein S28-2) (P34789)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm.
Interaction partners:
- Small ribosomal subunit protein eS10z
- Large ribosomal subunit protein uL4y
- Small ribosomal subunit protein eS21z
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS21y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein uS15z
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS6y
Sequence:
MDSQIKHAVVVKVMGRTGSRGQVTQVRVKFTDSDRFIMRNVKGPVREGDVLTLLESEREARRLR