wanglab/gogpt-training-data huggingface dataset:
Protein: Galactoside alpha-(1,2)-fucosyltransferase 2 (Alpha(1,2)FT 2) (Fucosyltransferase 2) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2) (SE2) (Secretor blood group alpha-2-fucosyltransferase) (Secretor factor) (Se) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.344) (Q10981)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs (By similarity). Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi.
Interaction partners:
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5
- Alpha-
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Exocyst complex component 6
- Beta-1,3-galactosyltransferase 5
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
Sequence:
MLVVQMPFSFPMAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQLRGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATASRIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQKFLRGLQVNGSRPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSLIFVVTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTGGDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH
Protein: Nicotinic acetylcyoline receptor Dalpha 4 subunit (Q9NFR4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
ADGHYEVTLMTKAIVYNNGLVIWQPPAVYKSSCSIDVEYFPYDVRTCILKLGSWTYDGFK
Protein: UNC93-like protein MFSD11 (Major facilitator superfamily domain-containing protein 11) (Protein ET) (O43934)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Molybdate-anion transporter
Sequence:
MSPESKKLFNIIILGVAFMFMFTAFQTCGNVAQTVIRSLNRTDFHGSGYTSMAIIYGVFSASNLITPSVVAIVGPQLSMFASGLFYSMYIAVFIQPFPWSFYTASVFIGIAAAVLWTAQGNCLTINSDEHSIGRNSGIFWALLQSSLFFGNLYIYFAWQGKTQISESDRRTVFIALTVISLVGTVLFFLIRKPDSENVLGEDESSDDQDMEVNESAQNNLTKAVDAFKKSFKLCVTKEMLLLSITTAYTGLELTFFSGVYGTCIGATNKFGAEEKSLIGLSGIFIGIGEILGGSLFGLLSKNNRFGRNPVVLLGILVHFIAFYLIFLNMPGDAPIAPVKGTDSSAYIKSSKEVAILCSFLLGLGDSCFNTQLLSILGFLYSEDSAPAFAIFKFVQSICAAVAFFYSNYLLLHWQLLVMVIFGFFGTISFFTVEWEAAAFVARGSDYRSI
Protein: Plant cysteine oxidase 1 (AtPCO1) (EC 1.13.11.20) (Hypoxia-responsive unknown protein 29) (Q9LXG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of N-terminal cysteine residues (N-Cys), thus preparing the protein for N-end rule pathway-mediated proteasomal degradation, upstream of the N-end rule enzymes ATE1, ATE2 and PRT6. Controls the preparation of the group VII ethylene response factor (ERF-VII) proteins for degradation via the 26S proteasome N-end rule pathway. Acts as an oxygen sensor that controls the stability of ERF-VII proteins, which are stabilized in flooding-induced hypoxia, and regulate transcriptional adaptation to these adverse conditions. Not active on Cys located inside or at the C-terminus of a peptide. Acts redundantly with PCO2 to repress the anaerobic response.
Subcellular location: Nucleus {ECO:0000269|PubMed:24599061}. Cytoplasm {ECO:0000269|PubMed:24599061}.
Interaction partners:
- E3 ubiquitin-protein ligase PRT6
- Sequence-specific DNA binding transcription factor
- Ethylene-responsive transcription factor RAP2-12
- Arginyl-tRNA--protein transferase 2
- LOB domain-containing protein 41
- Anaerobic nitrite reductase AHB1
- At4g33560
- Rhodanese-like domain-containing protein 17
- At5g66985
- Pyruvate decarboxylase 1
Sequence:
MGFEMKPEKEVLELISSKNQCKSNPNSVKKKNKNKNKKMMMTWRRKKIDSPADGITAVRRLFNTCKEVFSNGGPGVIPSEDKIQQLREILDDMKPEDVGLTPTMPYFRPNSGVEARSSPPITYLHLHQCDQFSIGIFCLPPSGVIPLHNHPGMTVFSKLLFGTMHIKSYDWVVDAPMRDSKTRLAKLKVDSTFTAPCNASILYPEDGGNMHRFTAITACAVLDVLGPPYCNPEGRHCTYFLEFPLDKLSSEDDDVLSSEEEKEGYAWLQERDDNPEDHTNVVGALYRGPKVED
Protein: BTB domain-containing protein (H2KZE7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSTERLMYLDLNKGNQIAMVIPSTRKGHAASRDNFGNSNHHGDEIVHRLNNGRRSEIDEVKPDLVSGAGDTVIKLNVGGTSFRIRISSIFARSADEKLSAFAQLNHEQRLQACDAFLMPQEEYYLERSAVLFDSIFKYYISGQLHRPLDVCPTEFATELAYWKINDGLMSNCCWRGYNMSPSLEELVAPKEKKIELHDRSMRSRIHQFCEGDGSLFSTLFTFGSITFVLISVIGLVLGSIHEFQVPIYKKGGKSERISNWSIVENENIIWEPHPIFGYVETVCIIWFTVEFIVRLAVTPNRFQFLVGIMNIVDMIAIIPFYLELGLALFGIDVASLSDIKGALLVVRVLRVLRVVRILKLGRYSSGMRTFALTLKSSARQLGMMGMVLSTGVVFFSTLLYFVEKDEKDTPFTSIPAAFWWAIVTMTTVGYGDYVPVTVPGKLIASGAIISGVLVLALPITIIVDNFMKVSGNVNANIFSSANQRPIDVAE
Protein: Vascular-related unknown protein 1 (Q9LSZ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of xylem development and growth. May regulate secondary wall formation during vascular development by modulation of brassinosteroid, gibberellin and auxin hormone signaling pathways.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24567189}. Nucleus {ECO:0000269|PubMed:24567189}.
Interaction partners:
- AT-hook motif nuclear-localized protein 24
- AT-hook motif nuclear-localized protein 29
- Protein RALF-like 16
- Protein RALF-like 7
Sequence:
MMDTFSCNSYEQNHPHDDDIDIDAHDHDSHGGDHQEESGWTTYLDDFSNQYRTTHHEENDHQDKSSYSLLATSTSLVSDAATHAFSGKSFPVNFPAKLKFGRGRTKKICEDDSLEDTASSPVNSPKVSHFEHIQTPPRKIEDYVSSSFVMGNIRGMGDHQIQIQEGGEQKVTLMRNLIDGNNNNNNNNMDLRSRGLCVVPISMLANFNGRC
Protein: T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) (O77323)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- T-complex protein 1 subunit delta
- CCT-beta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- Phosducin-like protein 1, putative
- Prefoldin subunit 4
- Serine/threonine-protein phosphatase
Sequence:
MSHLMSLPIVLLKEGTDTAQGRSQIIRNINACQIIVDIVKTTLGPRGMDKLIYTERDVTITNDGATVMNLLNISHPAASILVDIAKSQDDEVGDGTTSVVVVAGELLNEAKGLLNDGIEPNMIIDGFRNACNVAINKLNELSLNFSNKNEEEKRSILLKCAQTALNSKLVSNHKEFFGELVVNAVYKLGDNLDKSNIGIKKVTGGSCLDTQLIYGVAFKKTFSYAGFEQQPKKFINPKILLLNVELELKAEKENAEVRIENPNEYNSIVQAEWDIIFKKLNLIKDCGANIVLSKLPIGDIATQFFADHDIFCAGRVEDADLKRTANATGALVQTSLFNLNDDVLGTCGVFEEVQIGNERYNIFKECLKTKSVTIILRGGAKQFIEEVERSINDAIMIVLRCITNSEIVPGAGSIEMQLSKYLRIYSRSICNKEQIVLFSFAKALESIPRHLSHNAGYDSTDILNKLRKKHSEQTSDIWYGVDCMEGDIINAYDNCIFEVTKIKRNVIYSATEAACLILSIDETIKNPSSAAGTQRSPYS
Protein: Acetylpolyamine amidohydrolase 2 (APAH 2) (EC 3.5.1.-) (Acetylcadaverine deacetylase) (Acetylpolyamine deacetylase) (Acetylputrescine deacetylase) (EC 3.5.1.62) (Q9I6H0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the deacetylation of acetylated polyamines such as N-acetylputrescine and N-acetylcadaverine. Plays an important role in the metabolism of acetylated polyamines in P.aeruginosa. Is involved in the degradation pathways of N-acetylputrescine and N-acetylcadaverine, that allow P.aeruginosa to utilize these acetylpolyamines as a carbon source under glucose starvation. Shows nearly no activity against N(1)-acetylspermine and N(1)-acetylspermidine. Can also hydrolyze artificial trifluoroacetylated lysine-derivative, and to a lesser extent, acetylated lysine-derivative.
Interaction partners:
- Probable transcriptional regulator
- Probable transporter
- HTH-type transcriptional regulator ArgP
- Tryptophan 2-monooxygenase
- Uncharacterized protein
- Exotoxin A regulatory protein
Sequence:
MLTIYSDDHRLHHGRHELIGGQFTPCFEKPSRADMVLDRVKAVGLGEVRAPRDFGLEPIRRVHSEGFVRFLQNAWQDWLATGRSHDMLPIAWPTRRLRQTEPDNIDGRLGYYSFDAGAPITAGTWQAITSSANVALSGQSELANGARSVFSLCRPPGHHAAADYMGGYCFFNNAAIAAQAFLDRGAGRVAILDVDYHHGNGTQDIFYDRADVLFTSIHGDPRFEYPYFLGYADEKGNGVGTGYNFNYPLAAGSDWATWSQALQAAIRQIQAYAADALIVSLGVDTFKEDPISQFRLDSPDYLRMGEAIGKLGLATLFVMEGGYAVEEIGINAVNVLQGFEGVHR
Protein: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase (HMPDdc) (EC 4.1.1.51) (Q988D0)
Organism: Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099))
Function: Involved in the catabolism of pyridoxal 5-phosphate (Vitamin B6). Catalyzes the decarboxylation of 3-hydroxy-2-methylpyridine-4,5-dicarboxylate to yield 3-hydroxy-2-methylpyridine-5-carboxylate. The decarboxylation proceeds by an aldolase-like mechanism in which the binding of the substrate frees Glu-73 residue from its interaction with manganese ion replacing it by an interaction with the hydroxyl group from the substrate. Glu-73 residue then provides the proton for the keto-enol tautomerization. The decarboxylation reaction is analogous to the retroaldol reaction except that it does not need a base as the carboxylate is likely to be deprotonated under the reaction conditions.
Interaction partners:
Sequence:
MRRKVFEELVTATKILLNEGIMDTFGHISARDPEDPASFFLAQKLAPSLITVDDIQRFNLDGETSDNRPSYLERYIHSEIYKTRPDVQCVLHTHSPAVLPYCFVDTPLRPVTHMGAFIGESVPVYEIRDKHGDETDLFGGSPDVCADIAESLGSQTVVLMARHGVVNVGKSVREVVFRAFYLEQEAAALTAGLKIGNVKYLSPGEIKTAGKLVGAQIDRGWNHWSQRLRQAGLA
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IBX3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MARPGSGGGGSSQDAKHVLDEIGQQVHDQVEKEAKERSNGDLKGNLTISTIFDTETTGTDDPCSSDYTTRFDARGDPCKKDGTGNDVERFSVKQGAECGNSKIHGNSKGGTGTEVGACAPYRRLNLCNKNLENINKYDNTKAKHDLLAEVCHAAKYEGASITLHYPQYQNKYDDSGSTMCTMLARSFADIGDIIRGKDLYLGKKKKKQNGKETEREKLEDNLRKIFENIKKENNSKLKSLTDDQIREYWWTENRETVWKAMTCSEDLKNSSYFHATCIDGKNQSQARNQCRCPKTSGNVNIVPTYFDYVPQYLRWFEEWAEDFCRKKKKKVQNLQKQCRDKYQGDDRYCSRNGYDCEQTINKIGKLVIGKGCINCLYACNPYVDWINNQKEQFDKQVKKYGTEISDGGSGSGAAGGGGGRKKRGTSTTNYDGYESKFYKIFKGKCGTVDAFLGLLNNEKACKEVKDGGKIHFEKVNSTSGGTAGSNKTFYHSEYCQPCPLCGVKKKDGGNEWEKKKEDEKCNIKLYKPKDGVVGTTINFLYSGDETNEIEKKLKKFCRTENGTGDSNSDPSLYDPWQCYHVKQLEKDKEGVDDPVYEANVKNGGGLCILPNPKKNQDSGNNSSNEPEQFQKTFNNFFNFWVAHMLKDSIYWRTKKLVKCLKNGNTIKCGMNCKDDCGCFKRWVEKKQQEWGEIKEHFGKQDFGKQGENGVGEMLGVLMKSPSYVLKFVLEKDVLLTSIKSGYGKPEDIERIEELLKEEKKKNEEEAADGTDNENKTTIDKLLKHELTDAKDCQQKCDKKPPPPETPARNLPPPDTQRDPNQEESEEEEEEEDEDAPDDGEVDGDKGDGQETEPEEEEDTEDAKVEPAKDTTEDTEQDGQGPPVKKDEVNPCDIVSKLFQNPNNFSDACTLKYVTGKNYGWKCVSSGNGTTSSEGRSPRVARSAPSGDKDGAICVPPRRRRLYVGRLTKWAESKQVTQPQEDGKAPLAPTPPTSSGSQSDPLLTAFVESAAIETFFLWHKYKVDKIREEKEQQELFTNTSTLGKELQDKLERGNIPTDFLRQMFYTLGDYRDILFSGSKDAKNGVNDIFSGDKEMKEKEEKIKGAIQTFFENGASQPPSGKRNDKHEEWWKNHGEHIWNGMICALTYKDNDAKGQTPTQIQEVRDNLWDSGKNEPKKPQYQYQTAKLEEKNSGTKPTNQTPSSTSDNTPTTLTDFISRPPYFRYLEEWGQNFCKERKKRLAQIKHECMDGDTQKYSGDGEYCEEIFSKKYNVLQDLSSSCAKPCRLYKTWIEKKKTEYEKQKKAYEEQKSNYENEQKDKCQTQSNNNANEFSRTLGASPTAAAFLNRLGSCKNDNVEDNGEDKLDFNNPEQTFRPATNCGPCPVIGVKCKNGNCSDTSNGNMCKGGMITAENINNSTDDVSMLVSDNSTTGFNGLDEACQGAGVFEGIKEDKWKCGTVCGVDICTLEKKDTNGQEGDKKYITMKELLKRWLEYFFEDYNRIQKKLKPCTKSENKSTCIKGCVEKWIDKKKEEWKNINNNYLQQYKYVGNTLTNFLEILIPKIDLTNDKKKIKDLPAFLKLYGCNCADNSQNSTQNDVVLCLLENLKTKAKKCEENHKPSGNQQQPCQESPSVEDDEEDLTLEETEENTEEAKKKMMPTICETVVPTEPEEPGETCTPAAAGGGHNPEQTPVLKPEEEAPTPEAETKKDKAPVKPPSQPTTPQIVDKTPALVTSTLAWSVGIGFAAFTYFFLKKKTKASVGNLFQILQIPKSDYDIPTLKSKNRYIPYRSGTYKGKTYIYMEGETSGDDDKYAFMSDTTDITSSESEYEELDINDIYVPGSPKYKTLIEVVLEPSGNNTTASGKNTPSDTQNDIQNDGIPSSKITDNEWNTLKDDFISNMLQNEPNDIPNDYSSGDIPFNTQPNTLYFDNNQEKPFIMSIHDRNLYTGEEYNYNVNMSTKNVDIPMSDKNDVYSGIDLINDSLNSNNVDIYDEVLKRKENELFGTNHPKHTNTHSVTKSSNSDPIDNQLNLFHKWLDRHRDMCEQWNNKEKVLDKLKEEWNKDNNSGDIHTSDSNKTLNTDVSIQIHMDNPKPKNEFKNMDTTPNKSTMDTMLDDLEKYNEPYYYDFYKNDIYYDVNDDDKTSMDNNNNLVDKNNPVDSNNSTYNHRNPADINKTFVDINNHNQHPIEKPTKIQIEMNSNNREVVEQQYPIADIWNI
Protein: Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1) (Mitochondrial tyrosyl-tRNA synthetase) (Tyrosyl-tRNA synthetase) (TyrRS) (Q9W107)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9Y2Z4}.
Interaction partners:
- Tyrosine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- leucine--tRNA ligase
- Glycine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- leucine--tRNA ligase
- Probable proline--tRNA ligase, mitochondrial
- histidine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, mitochondrial
Sequence:
MLPLRRSLLKPLQDVLRHSHRQMSQKNLLELTDRGFFHGIFPDTAAPRMKQLFTRGQQSIYAGFDPTADSLHVGNLLVIMGLIHCQRAGHRPIALVGGATGLIGDPSGRKTERNQLGETVIETNLKAIEQQLRRVFENHENCLWDSKKQKLPLAPLIIVNNADWYADLQLIDFVANMGRHFRMGSMLSRSSVQSRLESEDGMSFTEFTYQIFQAYDWLHLLRRHNCCFQMGGSDQTGNLMTGHELISRVERKREVFGLTLPLVTTEEGDKFGKSAGNAVWLDGNKTSPFALYQFFLRMPDSEVEKLLKLFTFIPLPQVEQLMREHTKEPEKRKAQTLLAEDVTLLVHGESGLKQAERVTNALYKGNVEGLAELNLSEIQQTFQGATMVNLLTEPGMSILELAMKAKCFPTETDAVRIINAGGFYVNQKRVQNIAEVLTTGVHILRNGISLLRVGKRNFYIVRWQ
Protein: Pescadillo homolog (Nucleolar protein 7 homolog) (Q59X38)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome (By similarity). Required for the transition from hyphal to yeast growth.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03028}.
Interaction partners:
- Ribosome biogenesis protein ERB1
- RNA-binding GTPase
- Nucleolar GTP-binding protein 1
- rRNA-processing protein EBP2
- Ribosome biogenesis protein YTM1
- mRNA-binding ribosome synthesis protein
- ATP-dependent RNA helicase HAS1
- rRNA-binding ribosome biosynthesis protein
- Ribosome assembly factor mrt4
- AdoMet-dependent rRNA methyltransferase SPB1
Sequence:
MARIKKRGTTGNAKNFITRTQAIKKLQISLADFRRLCIFKGIYPREPRNKKKANKGSTAPVTFYYSKDIQYLLHEPVLDKFRQHKTFAKKLQKALGRGEVSDAYKLDQHRPKYTLNHIIKERYPTFADALRDLDDPLNMLFLFANMPATDKVSAKVVSEAEKLCNQWLAYVAKERCLKKVFVSIKGVYYQATVKGQEIRWLIPYKFPTNIPTDVDFRIMLTFLEFYSTLVHFVLYKLYNEAGLIYPPIIEKSIGLSGYVLQDKDAPLKKKEEKNDEEGKNLSKKELNKAIKADQEQQENDEQDNNNGESVEDIELDEFTSTKEDSLLQPSKYASSTAELFSKFIFYIGREVPLDILEFCILSCGGKIISEIAIDDLKINDPEAYKKLNLSNITHQIIDRPKILQKVPGRTYVQPQWVFDSINKQELINVNEYAAGETLPPHLSPWGDAGGYDPNKEVEKEDGEAEEDTDEEEEEVEIEDGDEDQEDEEEEEDEDLKAQKELELEAAGVKFSEINEEDKKSHSKKSKGTSNKEADEEKELKKIMMSNKQKKLFKKMQYGIEKKENREKQLTKKKKQLNKKKEQLKKLN
Protein: AT5g11480/F15N18_70 (P-loop containing nucleoside triphosphate hydrolases superfamily protein) (Putative GTP-binding protein) (Q9LYE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Short integuments 2, mitochondrial
- Protein Iojap-related
- Large ribosomal subunit protein uL24c
- At4g38020 family protein)
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- Pseudouridine synthase family protein
- Large ribosomal subunit protein bL21c
- Large ribosomal subunit protein uL13c
- Large ribosomal subunit protein uL3c
Sequence:
MILAHLPRFHLSILAKPSFSLSSSHFSFLNPKPSVTVSRTLFSFASKSNLATVEPIPLSVSDSTDLDDAPVEIALDKLFIPPETDISGEDSASLTTRILKGSNIVLSKYARDAQVVQADYVKSSVKTEDCPADGLPEFALVGRSNVGKSSLLNSLVRRKRLALTSKKPGKTQCINHFRINDKWYLVDLPGYGYASAPHELKQDWNKFTKDYFLNRSTLVSVFLLVDASIPVKPIDLEYASWLGQNQVPMTLIFTKCDKRKKKKNGGKKPEANIKEFQDLIQGFFETTPPWIMTSSVTNQGRDEILLHMAQLRNYWLKH
Protein: EF-hand domain-containing protein (A0A060Z1U0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- Myosin light chain 12A
- EF-hand domain-containing protein
- EF-hand domain-containing protein
Sequence:
VLFKVYSFYRRQCTGLDNPYLIRTKNSIKALEACTVCPVSLARSLLTSAHIDVAVGILATWPRKKVEPKKVEPKKPEPKAEAKAEPAKAPVPEPPKEPEVDLKSIILDFTLDQIEEFKEAFTLFDETPTGEMKIRYAQCGDLMRALGHNPTNTDVLKLLGKPKAEEMNSKLVDFETFLPMLQHISRTKETGTFEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKLMESEVDQLMIGQEDSSGHINYTEFVKHILST
Protein: Sarcoplasmic/endoplasmic reticulum calcium ATPase regulator ARLN (SERCA regulator ARLN) (Allregulin) (Another-regulin) (ALN) (Hepatitis C virus F protein-transactivated protein 1) (HCV F-transactivated protein 1) (Q8WVX3)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99M08}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Endoregulin
Sequence:
MEVDAPGVDGRDGLRERRGFSEGGRQNFDVRPQSGANGLPKHSYWLDLWLFILFDVVVFLFVYFLP
Protein: Probable ATP-dependent kinase TDA10 (EC 2.7.-.-) (Topoisomerase I damage affected protein 10) (P42938)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent kinase whose specificity is not yet known.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- D-3-phosphoglycerate dehydrogenase 2
- Glyoxylate reductase 1
- D-3-phosphoglycerate dehydrogenase 1
- Phosphoglycerate mutase 2
- Fatty aldehyde dehydrogenase HFD1
- Potassium-activated aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase [NAD
- Aldehyde dehydrogenase [NAD
- Magnesium-activated aldehyde dehydrogenase, cytosolic
- Phosphoglycerate mutase 3
Sequence:
MCDKSKTVLDYTIEFLDKYIPEWFETGNKCPLFIFFSGPQGSGKSFTSIQIYNHLMEKYGGEKSIGYASIDDFYLTHEDQLKLNEQFKNNKLLQGRGLPGTHDMKLLQEVLNTIFNNNEHPDQDTVVLPKYDKSQFKGEGDRCPTGQKIKLPVDIFILEGWFLGFNPILQGIENNDLLTGDMVDVNAKLFFYSDLLWRNPEIKSLGIVFTTDNINNVYGWRLQQEHELISKVGKGMTDEQVHAFVDRYMPSYKLYLNDFVRSESLGSIATLTLGIDSNRNVYSTKTRCIE
Protein: Frost (LP07623p) (Q9VH99)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RH02620p
- LD29830p
- GH07575p
Sequence:
MKVLTLILFTALVAVASGRPNGGWFGNFGSNWARRFGWGSGDDEIVQEQRWNSQNQWNPNGNGQGQWDGENGQGQSHGNNQGLGQGNGHGNNHHGHHGNSHGHGNGQGHGGQRPPPPPPTDLPELTTEDDVVSTTDVTSPAEETTLAPEVPEESTSQAPEEITTGSEEGSGSSEDTTTLAPEVPEESTTQAPEESTTDSEDGSGSEDTTQAPEETTTEEPEESTSEAPEESSSEAPEESTTEEPEESTTEAPVESTSEAPEESTTEAPEESTSEAPEESTIDSSAV
Protein: Protein dpy-30 homolog (Dpy-30-like protein 1) (Q9VKQ9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the SET1 complex that specifically di- and trimethylates 'Lys-4' of histone H3 and of the MLL3/4 complex which also methylates histone H3 'Lys-4'. Inhibits MTF-1 transcription factor activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:21694722}.
Interaction partners:
- Retinoblastoma-binding protein 5 homolog
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Histone-lysine N-methyltransferase SETD1
- Protein will die slowly
- WD repeat-containing protein 82
- CXXC-type zinc finger protein 1
- Host cell factor
- Histone-lysine N-methyltransferase trr
- PAX-interacting protein 1
- LD02225p
Sequence:
MEAKTDAPISPAPTTNPPAEAGKEPNASSNAQANPTAAPGAPPSGAIAVGQSTNPVAQQQQQPAVAKKPSSETNNMPTRQYLDQTVAPVLLHGMQALARERPTDPIQFLASYLLKHSNGCDENNASAAAVDNNS
Protein: tRNA methyltransferase 10 homolog B (EC 2.1.1.221) (RNA (guanine-9-)-methyltransferase domain-containing protein 3) (tRNA (guanine(9)-N(1))-methyltransferase TRMT10B) (Q6PF06)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in tRNAs. Probably not able to catalyze formation of N(1)-methyladenine at position 9 (m1A9) in tRNAs.
Interaction partners:
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein mS25
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein bS16m
Sequence:
MDWKLEGSTQKVESPVLQGQEGILEETGEDGLPEGFQLLQIDAEGECQEGEILATGSTAWCSKNVQRKQRHWEKIVAAKKSKRKQEKERRKANRAENPGICPQHSKRFLRALTKDKLLEAKHSGPRLCIDLSMTHYMSKKELSRLAGQIRRLYGSNKKADRPFWICLTGFTTDSPLYEECVRMNDGFSSYLLDITEEDCFSLFPLETLVYLTPDSEHALEDVDLNKVYILGGLVDESIQKKVTFQKAREYSVKTARLPIQEYMVRNQNGKNYHSEILAINQVFDILSTYLETHNWPEALKKGVSSGKGYILRNSVE
Protein: Metal-regulatory transcription factor 1 (D3ZBT4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Proton-coupled zinc antiporter SLC30A1
- Metallothionein-1
Sequence:
MGEHSPDDNIIFFKGEEDDLTPHDKMLRFVDDNGLVPSSSGTVYDRTTVLIEQDPGTLEDDEDDVQCGEHLPFLVEGEEGFLIDQEAMSQGYVQHIISPDQIHLTINPGSTPMPRNIEGATLTLQSECPETKRKEVKRYQCTFEGCPRTYSTAGNLRTHQKTHRGEYTFVCNQEGCGKAFLTSYSLRIHVRVHTKEKPFECDVQGCEKAFNTLYRLKAHQRLHTGKTFNCESQGCSKYFTTLSDLRKHIRTHTGEKPFRCDHDGCGKAFAASHHLKTHVRTHTGERPFFCPSNGCEKTFSTQYSLKSHMKGHDNKGTAYSALPQHNGSEDTNHSLYLSELGLLSTDSELQENSSSTQDQDLSTISPAIIFESMFQNPDDPAIQDDPLHTAALIDSFNGDAESVSDVPPPAGNSASLSLPLVLQPGISEPPQPLLPASTPSAPPPAPSLGPGSQPAAFGSPPALLQPPEVPVPHSTQFAANHQEFLPHPQAPPQTIVPGLSVVAGAPASAATVASAVAAPAPPQSTTEPLPAMVQTLPLGANSVLTNNPTITITPTPNTAILQSSLVMGEQNLQWILNGATSSPQNQEQIQQASKVEQVYFTTAVPVASSTGSSVQQIGLSVPVIIIKQEEACQCQCACRDSAKERAAGRRKGCSSPPPPEPNPQPPDGPSLQLPP
Protein: Regulator of G-protein signaling rgs-7 (Protein C2-RGS) (Regulator of G-protein signaling c2) (Q8WQC0)
Organism: Caenorhabditis elegans
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunit egl-30 (G-alpha(q)), thereby driving it into its inactive GDP-bound form. May organize egl-30 into a stable multiprotein signaling complex, and thereby persistently inhibit egl-30 when triggered by calcium or phospholipids.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein alpha-16 subunit
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit beta-1
- Chaperone ric-8
- Abi_C domain-containing protein
- Guanine nucleotide-binding protein alpha-5 subunit
Sequence:
MSDEDADEYDDQSSISSVSDDDDFSGSESESYQDTTESTGPSEATTDEMLWGRRRAPVCGIAAQAVRRQILMNQQHEPNVLGNNKKVYQTFGSTPQLANERHKEMYSQIRRGDDSSFRSRDRFVPPRRPRMGYGSSDLSAIEEMSPIRSSTYSSSSEAHRLSSLRAQTEWKPQLTSTTTSFQPLSPMNHHDKENGPFKAPMSPVCSSTPRSQRMYRKNPKYRRQFGSSLQLSESRLEESTSQESERAVTPESWMEHNNENEHPDQMMFAKPKQGSFPRPEAFGLDNAYAKHKDIRGIIFLSMSLCGRRLTLNVQNAAYFCSAARPTSVCSYVSAVLCHRPSSQSSSSSRQYRQRPDECYRTRLVTNCNSPSFDESFYFTFSENCVRDLLIVTVYEMDSNNAEKKRILGCMTFPVSRILKKASQVVGDPFPHYRRQDPMEDVEINNEGFFLLNKDQGRKQNFPQRKVRRQTFYEDPAFTGVSSAGSSVISNNTGGQMTMASPRLSVPNELTMGDYYRSTGSSDMRGRSTNNLLDYTSASSSTNGSAGGPEKLKLHRATLPSITTTTSENNSDDAKSLSPEQSPTDHHFLCPDDNGGVYGAGPAHSAIKKSSVRRAASFTFSPKHSSSKTNLRQLNGREEDKEKKRFLGPISRTLSYLRSKMDLALSTSSLYPSRDDVRQWEISFESLLNNKFGCALFRQFLKKEFSDENMDFWLECEEFKKMKDGKKSTTQKAIEIYSEFVAEHSPKEVNLDSDTRAATKAAVEAGCKPDTFALAQSRVEQLMSKDSYRRFLRDRLFLDLLESYEITDKEDKPSSSKDKN