wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphoserine phosphatase (PSP) (PSPase) (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) (Q5M819)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L-serine to L-serine. L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator. May also act on O-phospho-D-serine.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78330}.
Interaction partners:
- Phosphoserine aminotransferase
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Alanine--glyoxylate aminotransferase
- Cystathionine beta-synthase
- D-3-phosphoglycerate dehydrogenase
- Serine racemase
- Serine dehydratase-like
- Threonine aldolase 1
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MVSHSELRKLFCSADAVCFDVDSTVIREEGIDELAKFCGVEAAVSEMTRRAMGGALPFKDALTERLALIQPSRDQVQRLLAEHPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVAAKLNIPTTNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIGFLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
Protein: Beta-galactosidase (Beta-gal) (EC 3.2.1.23) (Lactase) (P00722)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Lactose permease
- Galactoside O-acetyltransferase
- Galactokinase
- Lactose operon repressor
- Aldose 1-epimerase
- Evolved beta-galactosidase subunit alpha
- Alpha-galactosidase
- Glucokinase
- Uncharacterized protein YihR
- LexA repressor
Sequence:
MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLVWCQK
Protein: FRIGIDA-like protein 4b (Q940H8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Flowering time control protein FY
Sequence:
MESSPDPGELIKSSQPSFFEFQKQASLMTSCNLLWKELSEHFTSMEQNLMKKSEALRQMIETLDNQTQSSIELLKHREVTIDHSVEIAEGKVEERVRAALDSLEKARDCGDEDTGEVDDGDGLLSALKSLCLKMDARGFWGFVIARKKELENLRSQIPVALVDCVDPPKLVLEAVSEVFPVDKRGGGEKVSNDFGWACVVILESLIPVMVDPVMGKSRLLVTPSVKEKAKEIAETWKASLEERGGIENVKTPDVHTFLQHLVTFGIVKKDDLALYRKLVVGSAWRKQMPKLAVSVGLGDQMPDMIEELIIRGQQLDAVHFTFEVGLVHLFPPVPLLKAYLRDAKKATALITDDSNNSGRSAHLVARKEQSALRAVLKCIEEYKLEEEFPPENLKKRLDQLEKTKTEKRKPAVIPANKRTRASYSGPMPPAKAGRITNAYVSSFPPPPPTFIRSQSHSPQYGVPAYTTSPPTIYSNRSPPYQYSPEAVHGSYQTSPVSYPTAYGTYCSPVAAPPPPVYHPHPHHHHHIQHAYY
Protein: Ferrochelatase (EC 4.98.1.1) (A0A8I6GEM4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000607}.
Interaction partners:
Sequence:
MGLKPQPTGEGGLQRVSLPEEMLGKPPLPGVVYGSSRACQPWRCQSGPAVVATTEKAHHAKTTKPQAQPERRKPKTGILMLNMGGPETLGEVQDFLQRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIGGGSPIKMWTSKQGEGMVKLLDELSPDTAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNEVGRKPTMKWSTIDRWPTHPLLIQCFADHILKELDHFPEEKRSEVVILFSAHSLPMSVVNRGDPYPQEVGATVHRVMEQLGYPNPYRLVWQSKVGPVPWLGPQTDEAIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAQKCGAENIRRAESLNGNPLFSKALADLVHSHIQSNKLCSTQLSLSCPLCVNPVCRKTKSFFTSQQL
Protein: Sterol 14-alpha demethylase (EC 1.14.14.154) (Cytochrome P450 monooxygenase 51C) (Ergosterol biosynthesis protein cyp51C) (B8NUK6)
Organism: Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
Function: Cytochrome P450 monooxygenase involved in the biosynthesis of ergosterol (By similarity). The existence of several duplicated sterol 14-alpha demethylase genes could be a good strategy to modulate the composition and fluidity of the cell membrane (By similarity). Catalyzes C14-demethylation of erburicol to produce 4,4,24-trimethyl cholesta-8,24(28)-dien-3-beta-ol (By similarity). As a target of azole drugs, plays a crucial role in azole drug susceptibility.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Delta
- Delta
- Terpene cyclase/mutase family member
- Sterol 14-alpha demethylase
- Sterol 14-alpha demethylase
- Farnesyl-diphosphate farnesyltransferase, putative.
- 3-ketosteroid reductase.
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
Sequence:
MSWPRIGAYALLAFVAIMALNVTYQFLFRMLNKTRPPLVFHWIPFIGSTIHYGMDPYGFFFSCREKYGDIFTFILLGRPTTVYLGTQGNEFILNGKLKDVNAEEVYSPLTTPVFGSDVVYDCPNSKLIEQKKFIKFGLSQAALEAHVPLIEKEVEDYLAMSPNFHGTSGEVDIPAAMAEITIFTAGSALQGEEVRSKLTTEFAVLYHDLDKGFTPINFMLPWAPLPHNKKRDAAHARMRSIYIDIINKRRNAGDNVPEKLDMIGNLMQCTYKNGQPLPDKEIAHIMITLLMAGQHSSSSISSWIMLRLASQPAVVEELYQEQLANLERTGPNGSLAPLQYKDFDNLPLHQNVIRETLRLHSSIHSLLRKVKNPLPVPGTPYVIPTSHVLLAAPGVTALSDEYFPNAMAWDPHRWETQAPQENNKDDIVDYGYGAMSKGTSSPYLPFGAGRHRCIGEKFAYLNLAVIVATMVRHLRFSNLDGQTGVPDTDYSSLFSGPMKPARIRWERRAAKSG
Protein: DNA mismatch repair protein MSH2 (AtMSH2) (MutS protein homolog 2) (O24617)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Forms three different heterodimers: MutS alpha (MSH2-MSH6 heterodimer), MutS beta (MSH2-MSH3 heterodimer) and MutS gamma (MSH2-MSH7 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. MutS alpha and MutS beta recognize single base mismatches and trinucleotide insertion-deletion loops (IDL) in the DNA. MutS gamma recognizes specifically the T/G single base mismatch. Plays a role in DNA homologous recombination repair and has a broad range of anti-recombination effects. Can suppress recombination between divergent direct repeats in somatic cells and possesses an anti-recombination meiotic effect. Is involved in a UV-B-induced DNA damage response pathway.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA mismatch repair protein PMS1
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein MSH6
- DNA mismatch repair protein MSH3
- DNA mismatch repair protein MLH3
- DNA mismatch repair protein MSH7
- Exonuclease 1
- Proliferating cell nuclear antigen 2
- DNA mismatch repair protein MSH1, mitochondrial
- Exonuclease 1
Sequence:
MEGNFEEQNKLPELKLDAKQAQGFLSFYKTLPNDTRAVRFFDRKDYYTAHGENSVFIAKTYYHTTTALRQLGSGSNALSSVSISRNMFETIARDLLLERNDHTVELYEGSGSNWRLVKTGSPGNIGSFEDVLFANNEMQDTPVVVSIFPSFHDGRCVIGMAYVDLTRRVLGLAEFLDDSRFTNLESSLIALGAKECIFPAESGKSNECKSLYDSLERCAVMITERKKHEFKGRDLDSDLKRLVKGNIEPVRDLVSGFDLATPALGALLSFSELLSNEDNYGNFTIRRYDIGGFMRLDSAAMRALNVMESKTDANKNFSLFGLMNRTCTAGMGKRLLHMWLKQPLVDLNEIKTRLDIVQCFVEEAGLRQDLRQHLKRISDVERLLRSLERRRGGLQHIIKLYQSTIRLPFIKTAMQQYTGEFASLISERYLKKLEALSDQDHLGKFIDLVECSVDLDQLENGEYMISSSYDTKLASLKDQKELLEQQIHELHKKTAIELDLQVDKALKLDKAAQFGHVFRITKKEEPKIRKKLTTQFIVLETRKDGVKFTNTKLKKLGDQYQSVVDDYRSCQKELVDRVVETVTSFSEVFEDLAGLLSEMDVLLSFADLAASCPTPYCRPEITSSDAGDIVLEGSRHPCVEAQDWVNFIPNDCRLMRGKSWFQIVTGPNMGGKSTFIRQVGVIVLMAQVGSFVPCDKASISIRDCIFARVGAGDCQLRGVSTFMQEMLETASILKGASDKSLIIIDELGRGTSTYDGFGLAWAICEHLVQVKRAPTLFATHFHELTALAQANSEVSGNTVGVANFHVSAHIDTESRKLTMLYKVEPGACDQSFGIHVAEFANFPESVVALAREKAAELEDFSPSSMIINNEESGKRKSREDDPDEVSRGAERAHKFLKEFAAIPLDKMELKDSLQRVREMKDELEKDAADCHWLRQFL
Protein: Nuclear factor interleukin-3-regulated protein (E4 promoter-binding protein 4) (Embryo implantation-related NFIL3/E4BP4-like transcription factor) (O08750)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites (By similarity). Represses promoter activity in osteoblasts. Represses transcriptional activity of PER1. Represses transcriptional activity of PER2 via the B-site on the promoter. Activates transcription from the interleukin-3 promoter in T-cells (By similarity). Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock. Protects pro-B cells from programmed cell death. Represses the transcription of CYP2A5. Positively regulates the expression and activity of CES2 by antagonizing the repressive action of NR1D1 on CES2. Required for the development of natural killer cell precursors.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:11316793}.
Interaction partners:
- Nuclear receptor subfamily 1 group D member 1
- Period circadian protein homolog 2
- Period circadian protein homolog 3
- Basic helix-loop-helix ARNT-like protein 1
- Nuclear receptor subfamily 1 group D member 2
- Cryptochrome-1
- Eomesodermin homolog
- Circadian locomoter output cycles protein kaput
- Cryptochrome-2
- Neuronal PAS domain-containing protein 2
Sequence:
MQLRKMQTIKKEPAPLDPTSSSDKMLLLNSALAEVAEDLASGEDLLLNEGSMGKNKSSACRRKREFIPDEKKDAMYWEKRRKNNEAAKRSREKRRLNDLVLENKLIALGEENATLKAELLSLKLKFGLISSTAYAQEIQKLSNSTAVYFQDYQTSKAAVSSFVDEHEPAMVAGSCISVIKHSPQSSLSDVSEVSSVEHTQESPAQGGCRSPENKFPVIKQEPVELESFAREAREERGTYSTSIYQSYMGSSFSTYSHSPPLLQVHGSTSNSPRTSEADEGVVGKSSDGEDEQQVPKGPIHSPVELQRVHATVVKVPEVNPSALPHKLRIKAKAMQVKVEALDSEFEGMQKLSSPADAIAKRHFDLEKHGTSGMAHSSLPPFSVQVTNIQDWSLKSEHWHHKELSSKTQSSFKTGVVEVKDGGYKVSEAENLYLKQGIANLSAEVVSLKRFIATQPISASDSR
Protein: NADP-specific glutamate dehydrogenase (NADP-GDH) (EC 1.4.1.4) (NADP-dependent glutamate dehydrogenase) (P78804)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Glutamate synthase
- Glutamine synthetase
- Probable NAD-specific glutamate dehydrogenase
- Aspartate aminotransferase, mitochondrial
- Probable isocitrate dehydrogenase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Pyruvate carboxylase
- Hydrolase C26A3.11
- Putative alanine aminotransferase
- Probable delta-1-pyrroline-5-carboxylate dehydrogenase
Sequence:
MSTPYEPEFQQAYKEIVGSIESSKLFEVHPELKRVLPIISIPERVLEFRVTWEDDKGNCRVNTGYRVQFNSALGPYKGGLRFHPSVNLSILKFLGFEQIFKNALTGLPMGGGKGGSDFDPKGKSDNEIRRFSQAFMRQLFRYIGPQTDVPAGDIGVTGFVVMHMFGEYKRLRNEYSGVVTGKHMLTGGSNIRPEATGYGVVYYVKHMIEHRTKGAETLKGKRVAISGSGNVAQYAALKCIQEGAIVKSISDSKGVLIAKTAEGLVPEEIHEIMALKEKRASIADSASLCKKHHYIAGARPWTNVGEIDIALPCATQNEVSGEEAAALIKQGCRYVAEGSNMGSSAEAVEVFEKSRASGEGCWLAPGKAANAGGVAVSGLEMAQNAQFSTWTHAEVDAKLAGIMQNIFEQSTDVASKYCDSGSNNIPSLVDGANIAGFLKVATAMQAVGDWW
Protein: Probable ATP-dependent RNA helicase DHX40 (EC 3.6.4.13) (DEAH box protein 40) (Protein PAD) (Q8IX18)
Organism: Homo sapiens (Human)
Function: Probable ATP-dependent RNA helicase.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 7
- Peptidyl-prolyl cis-trans isomerase-like 4
- Serum paraoxonase/arylesterase 2
- Probable ATP-dependent RNA helicase DDX49
Sequence:
MSRFPAVAGRAPRRQEEGERSRDLQEERLSAVCIADREEKGCTSQEGGTTPTFPIQKQRKKIIQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRKVAAISVAQRVAEEMKCTLGSKVGYQVRFDDCSSKETAIKYMTDGCLLKHILGDPNLTKFSVIILDEAHERTLTTDILFGLLKKLFQEKSPNRKEHLKVVVMSATMELAKLSAFFGNCPIFDIPGRLYPVREKFCNLIGPRDRENTAYIQAIVKVTMDIHLNEMAGDILVFLTGQFEIEKSCELLFQMAESVDYDYDVQDTTLDGLLILPCYGSMTTDQQRRIFLPPPPGIRKCVISTNISATSLTIDGIRYVVDGGFVKQLNHNPRLGLDILEVVPISKSEALQRSGRAGRTSSGKCFRIYSKDFWNQCMPDHVIPEIKRTSLTSVVLTLKCLAIHDVIRFPYLDPPNERLILEALKQLYQCDAIDRSGHVTRLGLSMVEFPLPPHLTCAVIKAASLDCEDLLLPIAAMLSVENVFIRPVDPEYQKEAEQRHRELAAKAGGFNDFATLAVIFEQCKSSGAPASWCQKHWIHWRCLFSAFRVEAQLRELIRKLKQQSDFPKETFEGPKHEVLRRCLCAGYFKNVARRSVGRTFCTMDGRGSPVHIHPSSALHEQETKLEWIIFHEVLVTTKVYARIVCPIRYEWVRDLLPKLHEFNAHDLSSVARREVREDARRRWTNKENVKQLKDGISKDVLKKMQRRNDDKSISDARARFLERKQQRTQDHSDTRKETG
Protein: Selenocysteine lyase (EC 4.4.1.16) (H7C1N7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
XFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCNFSIRGPRLQGDGPSPWSFRV
Protein: Pentatricopeptide repeat-containing protein At4g18520, chloroplastic (Protein PIGMENT-DEFICIENT MUTANT 1) (Protein SEEDLING LETHAL 1) (Q0WNP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for proper chloroplast development. Involved in the regulation of plastid gene expression probably through regulation of plastid-encoded polymerase (PEP) dependent chloroplast transcription. Required for RNA editing of several chloroplastic transcripts, especially accD transcripts. Required for processing of the chloroplastic rpoA pre-mRNA (Ref.6, Ref.7). Required for the monocistronic rpoA transcript processing from the rpl23-rpl2-rps19-rpl22-rps3-rpl16-rpl14-rps8-rpl36-rps11-rpoA polycistron. Binds the intergenic sequence of rps11-rpoA for rpoA monocistronic RNA cleavage (Ref.7).
Subcellular location: Plastid, chloroplast {ECO:0000269|Ref.7}.
Interaction partners:
- Sulfate transporter 1.2
- Sel1 repeat protein
- Thioredoxin-like fold domain-containing protein MRL7, chloroplastic
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic
- Multiple organellar RNA editing factor 9, chloroplastic
- Multiple organellar RNA editing factor 2, chloroplastic
- AT4g27600/T29A15_90
- FG-GAP repeat-containing protein
- Multiple organellar RNA editing factor 8, chloroplastic/mitochondrial
Sequence:
MFSLSLIQPRLRISEIPVTQSYKSPTICYSSDSRTKREEQRHVRLPGFRLVSGKRASFDSGFSGFKGENVNQDDSSSFDSERVDYALLAEWLQSSNGMRLIKRIHAMALKCFDDQVIYFGNNLISSCVRLGDLVYARKVFDSMPEKNTVTWTAMIDGYLKYGLEDEAFALFEDYVKHGIRFTNERMFVCLLNLCSRRAEFELGRQVHGNMVKVGVGNLIVESSLVYFYAQCGELTSALRAFDMMEEKDVISWTAVISACSRKGHGIKAIGMFIGMLNHWFLPNEFTVCSILKACSEEKALRFGRQVHSLVVKRMIKTDVFVGTSLMDMYAKCGEISDCRKVFDGMSNRNTVTWTSIIAAHAREGFGEEAISLFRIMKRRHLIANNLTVVSILRACGSVGALLLGKELHAQIIKNSIEKNVYIGSTLVWLYCKCGESRDAFNVLQQLPSRDVVSWTAMISGCSSLGHESEALDFLKEMIQEGVEPNPFTYSSALKACANSESLLIGRSIHSIAKKNHALSNVFVGSALIHMYAKCGFVSEAFRVFDSMPEKNLVSWKAMIMGYARNGFCREALKLMYRMEAEGFEVDDYIFATILSTCGDIELDEAVESSATCYLETS
Protein: Ubiquitin-conjugating enzyme E2 S (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme S) (Ubiquitin carrier protein S) (Ubiquitin-protein ligase S) (Q9VX25)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating polyubiquitin chains initiated by the E2 enzyme vih/UbcH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit.
Interaction partners:
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 4
- GEO06356p1
- Anaphase-promoting complex subunit 10
- Cell division cycle 16
- Cyclosome subunit 8
- E1 ubiquitin-activating enzyme
- Anaphase-promoting complex subunit 5
- Anaphase promoting complex subunit 7, isoform A
Sequence:
MSSQYSNVENLSPQTIRQVMRELQEMETTPPEGIKVLINESDVTDIQALIDGPAGTPYAAGIFRVKLTLNKDFPLTPPKAYFLTKIFHPNVAANGEICVNTLKKDWKPDLGIKHILLTIKCLLIVPNPESALNEEAGKMLLERYDDYSQRARMMTEIHAQPAKCGVGAVGDAKDDGGPSTKKHAGLDKKLQDKKKEKLLKEKKRMLKRL
Protein: APC membrane recruitment protein 1 (Amer1) (Protein FAM123B) (F1RDM5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Detected in nuclear paraspeckles that are found close to splicing speckles. Translocates to the cell membrane following binding to PtdIns(4,5)P2 (By similarity). {ECO:0000250}.
Interaction partners:
- Axin-1
- Catenin beta-1
- APC regulator of WNT-signaling pathway
- Glycogen synthase kinase-3 beta
- Casein kinase I isoform alpha
- Dipeptidyl peptidase 3
- APC regulator of WNT-signaling pathway 2.
- F-box and WD repeat domain-containing 11-B
- F-box and WD repeat domain-containing 11-A
Sequence:
MEIATRCEVGAMRGPSSDSVSHDIPQPQSPPSVKIRKTAFKFFGGRKSICVLPSFFGGRGRSQRKGSSKTGVTKSQTYDGVSRACWDDLGRSSSEVASGDFEFCSEPQKSQEDHGKSQSLPRQRRGLRGLFSSIRRHRKNKNVEVEKREALEMSSSFHAKTVPGALPSVSDRGDYHGDSQGEELVPDVPNQTTGSECELPLAATECTIDVTLVPEKRRSRVEMDKRRRAEEEGIGEDEKTGRQEGLMTYHQPLSAESELDRLAEQNVDVPDGEPPVASCSSENLVFGDVSSLKSFDSLTGCGDIIADQDDVSVAESSVSADRGSRNAGKRSSCFVTYQGGGEEMATPDEIDADYLQSLWESETSNEVCYIPSDRGSDSPSLTPDQQLSSIRATSSSSPMGITETALTPADLLSPQSDRQESVPNSDEGYYDSTTPGMEEESRERPHQERLPRDSYSGDALYELFEPDDRLLSPSLPPKDAHSFVGAPLQADKSPTNPLYSLASTAIETGAMETEEERLSKIQHALLCCELQNLRSPSKNQLLFHSDCFYDDSNLPVDDSKQDLQEVINQRYPQSPPRSQAVKEGVPRIRGQVQESSLFAPCADSVLNPQVIETTRPQPQSDDQGSLRPSRGCSQSQEELMVCFSQALVDFTKNTRLYRNSTESLDGSESSSPFGPSLRALPAIVTFDVVDMENEGECEQQTDLAEEEEELASPYEPFEDDGCYLQQDAFAECDQRTFDAYEQSLLLSNAWGIASLPRHLSLGRPCPPVPAPLALNRRSRSLDTDSLEFQTSEIYTSVTKYDSKGTAFSQSRTVDCNDMDFPRQPCRITVDSWRRGYRQNFDSSNASQQELKLPHLSQSTVRPSHLPLKNNCRSRNLPAATRVDGEGEILFGGGDALYPCSYPPMGTQWKNRPVGVTQGVPHLRSEQSADH
Protein: Tyrosine-protein kinase JAK1 (EC 2.7.10.2) (Janus kinase 1) (JAK-1) (P52332)
Organism: Mus musculus (Mouse)
Function: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor. Kinase partner for the type I interferon receptor IFNAR2. In response to interferon-binding to IFNAR1-IFNAR2 heterodimer, phosphorylates and activates its binding partner IFNAR2, creating docking sites for STAT proteins. Directly phosphorylates STAT proteins but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors.
Subcellular location: Endomembrane system; Peripheral membrane protein. Note=Wholly intracellular, possibly membrane associated.
Interaction partners:
- Signal transducer and activator of transcription 1
- Interferon lambda receptor 1
- Interleukin-10 receptor subunit alpha
- Interferon gamma receptor 1
- Interleukin-2 receptor subunit beta
- Interferon alpha/beta receptor 1
- Signal transducer and activator of transcription 3
- Cytokine receptor common subunit gamma
- Suppressor of cytokine signaling 3
- Ifngr2 protein
Sequence:
MQYLNIKEDCNAMAFCAKMRSFKKTEVKQVVPEPGVEVTFYLLDREPLRLGSGEYTAEELCIRAAQECSISPLCHNLFALYDESTKLWYAPNRIITVDDKTSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKRVPEATPLLDASSLEYLFAQGQYDLIKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVHDLKVKYLATLETSTLTKHYGAEIFETSMLLISSENELSRCHSNDSGNVLYEVMVTGNLGIQWRQKPNVVPVEKEKNKLKRKKLEYNKHKKDDERNKLREEWNNFSYFPEITHIVIKESVVSINKQDNKNMELKLSSREEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEVLGGQKQFKNFQIEVQKGRYSLHGSMDHFPSLRDLMNHLKKQILRTDNISFVLKRCCQPKPREISNLLVATKKAQEWQPVYSMSQLSFDRILKKDIIQGEHLGRGTRTHIYSGTLLDYKDEEGIAEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDALTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSDIGPFIKLSDPGIPVSVLTRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKQPTTEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICMEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAIQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLIQCKFYIASDVWSFGVTLHELLTYCDSDFSPMALFLKMIGPTHGQMTVTRLVKTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTTFQNLIEGFEALLK
Protein: Transcription factor Sox-1 (XlSox1) (xSox1) (SRY (sex determining region Y)-box 1) (Q2PG84)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional activator (By similarity). Participates in neural induction.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P48430, ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
Sequence:
MYSMMMETDLHSPGVQPPNNTGQGGGNKASQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLHAAGGGHMGVGLSPGGGGGGCGGAGGMVVQRMESPGSGASTGGYAHMNGWANGAYPGSVAAAAAAAMMQEAQLAYSQQQQQHPGSGGHHPHHHPHHPHHHPHHHPHHNPTSHPTPPQPMHRYDMSALQYSPLPGAQTYMSASPSSYGALSYSSSQQQHQGSPSSAAVAAAAAAASSGALGVLGSLVKSEPSVSPPVSGGGSHNRPPCPGDLREMISMYLPGGGEAGDPAAAAAAAAAAAAATSRLHSLPQHYQGTGTGITSTMPLTHI
Protein: Replication protein E1 (EC 3.6.4.12) (ATP-dependent helicase E1) (P17382)
Organism: Human papillomavirus 31
Function: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000}.
Interaction partners:
Sequence:
MADPAGTDGEGTGCNGWFYVEAVIDRQTGDNISEDENEDSSDTGEDMVDFIDNCNVYNNQAEAETAQALFHAQEAEEHAEAVQVLKRKYVGSPLSDISSCVDYNISPRLKAICIENNSKTAKRRLFELPDSGYGNTEVETQQMVQVEEQQTTLSCNGSDGTHSERENETPTRNILQVLKTSNGKAAMLGKFKELYGVSFMELIRPFQSNKSTCTDWCVAAFGVTGTVAEGFKTLLQPYCLYCHLQSLACSWGMVMLMLVRFKCAKNRITIEKLLEKLLCISTNCMLIQPPKLRSTAAALYWYRTGMSNISDVYGETPEWIERQTVLQHSFNDTTFDLSQMVQWAYDNDVMDDSEIAYKYAQLADSDSNACAFLKSNSQAKIVKDCGTMCRHYKRAEKRQMSMGQWIKSRCDKVSDEGDWRDIVKFLRYQQIEFVSFLSALKLFLKGVPKKNCILIHGAPNTGKSYFGMSLISFLQGCIISYANSKSHFWLQPLADAKIGMLDDATTPCWHYIDNYLRNALDGNPVSIDVKHKALMQLKCPPLLITSNINAGKDDRWPYLHSRLVVFTFPNPFPFDKNGNPVYELSDKNWKSFFSRTWCRLNLHEEEDKENDGDSFSTFKCVSGQNIRTL
Protein: NDRG family member 4 (Ndrg4) (A6XCT1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPECWDGEHDIETPYGMLHVVIRGAPKGNKPAILTYHDVGLNHKLCFNSFFQNEDMLEITKHFVVCHVDAPGQHIGAPQMPQGYQYPTMDQLAGMLPSVVQHFGFKSIVGIGVGAGAYILAKFALIFPDLVEGLVLLNIDPNGKGWIDWAATKLSGLTSTLPDTVLTHLFSQEELMSNTEVVQNYRQQINNTINQFNLQLFWNMYNSRRDLEMNRSGSVINAKTLRCPVMLVVGDNAPAEEGVVECNSKLDPTNTTFLKMADSGGMPQITQPGKLTEAFKYFLQGMGYMPSASMTRLARSRTASLTSAGSVDGSRNRACTHSDSSEGVGQVSHTMEVSC
Protein: Homeobox protein engrailed-like (Q5BJ08)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- PR domain zinc finger protein 12
- Transporter
- Vesicular glutamate transporter 2.1
- PR domain zinc finger protein 13
Sequence:
MDEQKDQNSRDSTESESVSLSPNIPSPPILPHQAAQQAHRTTNFFIDNILRPDFGCKKDPGSRDRAQTSGRENVNPMVIRPSHNSSLCQDSNCSSDSTSSSSSSSPSSKQSSVKHFEGNGSTAARNGENTPSIMMVNANGGTPPAKESQPLLWPAWVYCTRYSDRPSSGPRTRKLKKKKSEKEDKRPRTAFTAEQLQRLKAEFQANRYITEQRRQSLAQELNLNESQIKIWFQNKRAKIKKASGYKNGLALQLMAQGLYNHSTTTVQDEKEDSE