wanglab/gogpt-training-data huggingface dataset:
Protein: Polycomb group protein EMBRYONIC FLOWER 2 (Q8L6Y4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Polycomb group (PcG) protein. Involved in flowering processes by repressing unknown target genes and preventing reproductive development. Participates in polycomb group (PcG) protein complex-mediated (probably in complex with EMF1) silencing of the flower homeotic genes AGAMOUS (AG), PISTILLATA (PI), and APETALA3 (AP3), as well as of some regulatory genes such as ABSCISIC ACID INSENSITIVE3 (ABI3), LONG VEGETATIVE PHASE1 (LOV1), and FLOWERING LOCUS C (FLC) during vegetative development, by mediating trimethylation of histone 3 lysine 27 on the AG chromatin (H3K27me3). PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone-lysine N-methyltransferase CLF
- Histone-lysine N-methyltransferase EZA1
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- Histone-binding protein MSI1
- Histone-lysine N-methyltransferase MEDEA
- Lysine-specific demethylase ELF6
- WD-40 repeat-containing protein MSI5
- WD-40 repeat-containing protein MSI4
- Putative E3 ubiquitin-protein ligase RING1a
- Chromo domain-containing protein LHP1
Sequence:
MPGIPLVSRETSSCSRSTEQMCHEDSRLRISEEEEIAAEESLAAYCKPVELYNIIQRRAIRNPLFLQRCLHYKIEAKHKRRIQMTVFLSGAIDAGVQTQKLFPLYILLARLVSPKPVAEYSAVYRFSRACILTGGLGVDGVSQAQANFLLPDMNRLALEAKSGSLAILFISFAGAQNSQFGIDSGKIHSGNIGGHCLWSKIPLQSLYASWQKSPNMDLGQRVDTVSLVEMQPCFIKLKSMSEEKCVSIQVPSNPLTSSSPQQVQVTISAEEVGSTEKSPYSSFSYNDISSSSLLQIIRLRTGNVVFNYRYYNNKLQKTEVTEDFSCPFCLVKCASFKGLRYHLPSTHDLLNFEFWVTEEFQAVNVSLKTETMISKVNEDDVDPKQQTFFFSSKKFRRRRQKSQVRSSRQGPHLGLGCEVLDKTDDAHSVRSEKSRIPPGKHYERIGGAESGQRVPPGTSPADVQSCGDPDYVQSIAGSTMLQFAKTRKISIERSDLRNRSLLQKRQFFHSHRAQPMALEQVLSDRDSEDEVDDDVADFEDRRMLDDFVDVTKDEKQMMHMWNSFVRKQRVLADGHIPWACEAFSRLHGPIMVRTPHLIWCWRVFMVKLWNHGLLDARTMNNCNTFLEQLQI
Protein: Serine/threonine-protein kinase BRSK2 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 2) (BR serine/threonine-protein kinase 2) (Serine/threonine-protein kinase SAD-A) (D3ZML2)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-523' and 'Ser-573'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-175 can inhibit insulin secretion, BRSK2 phosphorylated at Thr-261 can promote insulin secretion. Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELGHLQLFGNPVSKVRSVAMELVILVQTLAYTSFRLLGTFLPVRYLRHSVLSRPPERARLVLRGAPCTHMGPVWNMVGMAYTQNPPIMGETGVYGSQWVMSSAPSKHYTSLGLSVPSPSCSLSPSLFPFCAPDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGKDMAKMGPPAARREQP
Protein: GTP-binding nuclear protein Ran (B5MDF5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363057}.
Interaction partners:
Sequence:
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQEMGIHHVAHAGLELMSSAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Protein: Autophagy protein 5 (Meiotically up-regulated gene 77 protein) (O74971)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with atg12, through a ubiquitin-like conjugating system involving atg7 as an E1-like activating enzyme and atg10 as an E2-like conjugating enzyme, is essential for its function. The atg12-atg5 conjugate acts as an E3-like enzyme which is required for lipidation of atg8 and atg8 association to the vesicle membranes (By similarity). Has a role in meiosis and sporulation.
Subcellular location: Cytoplasm. Nucleus. Preautophagosomal structure membrane; Peripheral membrane protein.
Interaction partners:
- Ubiquitin-like protein ATG12
- Autophagy-related protein 3
- Serine/threonine-protein kinase atg1
- Autophagy-related protein 8
- Ubiquitin-like modifier-activating enzyme atg7
- Putative lipase atg15
- Autophagy-related protein 18
- Autophagy protein 16
- Autophagy-related protein 9
- Probable cysteine protease atg4
Sequence:
MNVDNNKGNIPELLWNGTISVRIDYEGNSLAYLANVPRQSYFAQILPNVQRLLAPSIPLSECWLDYNGVPLKWHWPVGLLFDLLTVFDPDTPRAPVLWRIQLRSGLFPTTKILQMETMDTFRTYFFNCLKESDYVRNGSSSGIIALSKAETDTYWNAILNHDYYDFRPIAIKILFSKSKFIPLKIYLGANAPIIQTSAPLGSSLGEFLNKRLPDLFPSCDKFLIVKPVIHGITIFLQSVLDELNRDFCYIDGFLHIVLMKV
Protein: Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) (O74834)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03166}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:12810074}.
Interaction partners:
- Apurinic-apyrimidinic endonuclease 1
- DNA-
- Endonuclease III homolog lyase)
- Probable deoxyuridine 5'-triphosphate nucleotidohydrolase
- Adenine DNA glycosylase
- G/U mismatch-specific uracil DNA glycosylase
- Probable thymidylate synthase
- Actin-related protein 4
- Flap endonuclease 1
- Replication factor A protein 2
Sequence:
MTVLNTTDKRKADDTVNKLDGKLKQPRLDNFFKTNTSSPALKDTQVLDNKENNSVSKFNKEKWAENLTPAQRKLLQLEIDTLESSWFDALKDEFLKPYFLNLKEFLMKEWQSQRVFPPKEDIYSWSHHTPLHKTKVILLGQDPYHNIGQAHGLCFSVRPGIPCPPSLVNIYKAIKIDYPDFVIPKTGYLVPWADQGILMLNASLTVRAHQAASHSGKGWETFTSAVLQVALNRNRKGLVILAWGTPAAKRLQGLPLKAHYVLRSVHPSPLSAHRGFFECHHFKKTNEWLEEQYGPEKCINWSAVSEQKAKIKSSELESSSTE
Protein: Protein deadpan (Q26263)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional repressor of genes that require a bHLH protein for their transcription. In the larval brain, required to maintain the self-renewal and identity of type II neuroblasts by regulating the expression of the transcriptional repressor erm together with other self-renewal transcriptional repressors such as klu and E(spl)mgamma-HLH. As part of its role in neuroblasts development, has been shown to be a direct target of the Notch signaling pathway, however might work also independently of N/Notch. In the developing larval and pupal brain, required for mushroom body differentiation. Involved in sex determination and SXL transcription repression when in complex with the corepressor protein Groucho.
Subcellular location: Nucleus {ECO:0000269|PubMed:1427077}.
Interaction partners:
- Achaete-scute complex protein T8
- Protein groucho
- Worniu
- Inscuteable
- Fez family zinc finger protein erm
- Protein elav
- Protein sisterless A
- Achaete-scute complex protein T4
- Sphingosine-1-phosphate lyase
- Klumpfuss, isoform B
Sequence:
MDYKNDINSDDDFDCSNGYSDSYGSNGRMSNPNGLSKAELRKTNKPIMEKRRRARINHCLNELKSLILEAMKKDPARHTKLEKADILEMTVKHLQSVQRQQLNMAIQSDPSVVQKFKTGFVECAEEVNRYVSQMDGIDTGVRQRLSAHLNQCANSLEQIGSMSNFSNGYRGGLFPATAVTAAPTPLFPSLPQDLNNNSRTESSAPAIQMGGLQLIPSRLPSGEFALIMPNTGSAAPPPGPFAWPGSAAGVAAGTASAALASIANPTHLNDYTQSFRMSAFSKPVNTSVPANLPENLIHTLPGQTQLPVKNSTSPPLSPISSISSHCEESRAASPTVDVMSKHSFAGVFSTPPPTSAETSFNTSGSLNLSAGSHDSSGCSRPLAHLQQQQVSSTSGIAKRDREAEAESSDCSLDEPSSKKFLAGAIEKSSSAWRPW
Protein: Palmitoyltransferase PFA3 (EC 2.3.1.225) (Protein fatty acyltransferase 3) (P42836)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16186255}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16186255}.
Interaction partners:
- Vacuolar protein 8
- Palmitoyltransferase AKR1
- Probable palmitoyltransferase AKR2
- Ras modification protein ERF4
Sequence:
MNDRLSLTSLFPRCLTTCLYIWTAYITLTRIHQIPRWFLALTIVPTLAVALYTYYKVIARGPGSPLDFPDLLVHDLKAAENGLELPPEYMSKRCLTLKHDGRFRVCQVCHVWKPDRCHHCSSCDVCILKMDHHCPWFAECTGFRNQKFFIQFLMYTTLYAFLVLIYTCYELGTWFNSGSFNRELIDFHLLGVALLAVAVFISVLAFTCFSIYQVCKNQTTIEVHGMRRYRRDLEILNDSYGTNEHLENIFDLGSSMANWQDIMGTSWLEWILPIETFKYKKSKHTKDEKGLYFNVRPQVQDRLLSSRCLEDQLLRRVTPRPSLEADRASVEIIDAN
Protein: Peroxiredoxin-4 (EC 1.11.1.24) (Antioxidant enzyme AOE372) (AOE37-2) (Peroxiredoxin IV) (Prx-IV) (Thioredoxin peroxidase AO372) (Thioredoxin-dependent peroxide reductase A0372) (Thioredoxin-dependent peroxiredoxin 4) (Q13162)
Organism: Homo sapiens (Human)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18052930, ECO:0000269|PubMed:9388242}. Endoplasmic reticulum {ECO:0000269|PubMed:18052930}. Note=Cotranslationally translocated to and retained within the endoplasmic reticulum. A small fraction of the protein is cytoplasmic. {ECO:0000269|PubMed:18052930}.
Interaction partners:
- Thioredoxin domain-containing protein 5
- Endoplasmic reticulum resident protein 44
- Protein disulfide-isomerase A6
- Thioredoxin
- Peroxiredoxin-5, mitochondrial
- Glutamine synthetase
- Sulfiredoxin-1
- Glutathione peroxidase 3
- Protein disulfide-isomerase A3
- Protein disulfide-isomerase
Sequence:
MEALPLLAATTPDHGRHRRLLLLPLLLFLLPAGAVQGWETEERPRTREEECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN
Protein: RNA-binding protein NAB6 (Nucleic acid-binding protein 6) (Q03735)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein that associates with mRNAs encoding cell wall proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
- Eukaryotic peptide chain release factor GTP-binding subunit
- Heterogeneous nuclear rnp K-like protein 2
- mRNA-binding protein PUF3
Sequence:
MSNSNSKKPVANYAYRQQQDYNGMNAMVGNPMMYHPVDFVNGAGQYGPSQHPAYYTNSPLPNIPPTPFDTAYGASLFPSHLLMGSPFVSSPNMQSGYNSARSSNLKRKAYSRPVSNHNGYNGNSNSNQNNTNNGMVTPSNYYRMGRNSFSRNNNSTRNVTHNNNKGCDTRNNSGRRTFARNNIFDDILPEMLLQRPFCINYKVLPTGDDAYRTRSLLIENVDHSIDLHSIVKNFVKSNTLESAYLIEGGKSDDSKDVETKNLSILISFLTKGDCLNFYNNILQRLSEFKTFLKSEALNLKFVCLNYDPKCLPTFIESEALTENAEEADITNGSTMISASLHHNIANKDATRSIIIEFKSPVEKSDLFKKKLQFLDRSKNKRYILESIDLVNTDVPSNQFPENYAVLTFLNISMAIEVLDYLKKYSKNLGISKCFYVSLAPLVVSSARSSVANIYEGKTSTHRLSVPSVTAGNNNDSNNNGNNNKSNMSGITTLNNNSSIGVSVYGHSNMSLTSLSSSVSLNEEIDMLATKLQGVELDGTYLEINYRDYQTPTIEEHSTHLSNVKISKTTENSRQFSQDIPSPLPLNEHMFMNDSNQSNGAIIPQQLIATPSPVSPNLQMNQRVLPNPITQSLEQNFNVSAKVASSMGSDIGNRTIYIGNINPRSKAEDICNVVRGGILQSIKYIPEKKICFVTFIEAPSAVQFYANSFIDPIVLHGNMLRVGWGHYSGPLPKLISLAVTIGASRNVYVSLPEFAFKEKFIHDPQYKKLHETLSLPDAEQLREDFSTYGDIEQINYLSDSHCCWINFMNISSAISLVEEMNKESTVQNESGEVTLKRATEEKFGGRYKGLLINYGKDRCGNINKNLIAGKNSRFYKKVKRPSYNIRLSKLEEKRRQNEIDEKEKAFDKPLNLESLGISLDAHKDNGGGETGTANNTGHENESELEAENENGNETGSFGGLGLAVASSDVKRATSDETDYEDIFNKSSGSSDSSSDVEVIMHSPSDPEYALKSQTLRSSSQTVINSKRPVKIEDEEEAVGMSQLNYRSSLRQAPPRAPSTLSYNHSKNNETPMQDIFTNGETANNRKKKRGSFARHRTIPGSDVMAQYLAQVQHSTFMYAANILGASAEDNTHPDE
Protein: Membrane protein FAM174B (Q3ZCQ3)
Organism: Homo sapiens (Human)
Function: Essential for Golgi structural integrity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29851555}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus {ECO:0000269|PubMed:29851555}.
Interaction partners:
Sequence:
MRAVPLPAPLLPLLLLALLAAPAARASRAESVSAPWPEPERESRPPPGPGPGNTTRFGSGAAGGSGSSSSNSSGDALVTRISILLRDLPTLKAAVIVAFAFTTLLIACLLLRVFRSGKRLKKTRKYDIITTPAERVEMAPLNEEDDEDEDSTVFDIKYR
Protein: RE21313p (Q8SXU1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTPLQTRMALAEIPDRLEALRMANTPTNSNRRTPDEPTPAAIINTPNANGGLGLRVDNDVNVVQAQDFVFSPLPSPDELVIRQRGRRRFTTTYSQDKVNGGGGAGGGASGGSSMRSPFQRTPTKNFQLTSGMILRSSPRKRLTMGSTPPEPTPMDTYSPIKMATTKQLWPGTPVVKKLKMEDRPVGQTNTDATLPSLLQGLSQEQLIDLIMNNIKSASDEGEIRTQLPTPDISALEQDLHHAKRLIFKSLPTSRLCKKTDAAAYSKASMHLNEFKRVLQSQAKRLHDSTHWDALVDYVSMAWQCVASTPNWESHAHNAVRRQCFKLLACSCYAAIKHGGMRLGQLRLETLERNLREWSKDYEDVLSCVNALQRTLNSRSSL
Protein: ConoCAP [Cleaved into: ConoCAP-a (CCAP-vil); ConoCAP-b; ConoCAP-c] (E3PQQ8)
Organism: Conus villepinii (Villepin's cone)
Function: In contrast to other members of the CCAP family which are cardio-accelerators, conoCAP-a decreases the heart frequency in Drosophila larvae (26%), rats and zebrafish embryos. It also reduces the blood pressure in rats. It decreases systolic calcium in ventricular cardiac myocytes, indicating that it may act via impairment of intracellular calcium trafficking.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MVSLGHVLFVILLPVLLPVAADDPDDQMLSQISLPSSSRSEYDDNDVSKRVFCNGFTGCGGRHRDRSRRQERYGKRLIPVLAKRPFCNSFGCYNGKRSLSGAGPALSTPVDPSRNNKARTMARMLDAAASARHEQQQQLLQQREQRGLESRDPAASGDLSKRLFCNGYGGCRGGKRTLYSPWLERMNEVADDRSARNALCTRLGWRE
Protein: Sodium/potassium-transporting ATPase subunit alpha-2 (Na(+)/K(+) ATPase alpha-2 subunit) (EC 7.2.2.13) (Na(+)/K(+) ATPase alpha(+) subunit) (Sodium pump subunit alpha-2) (P06686)
Organism: Rattus norvegicus (Rat)
Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit beta-3
- Protein ATP1B4
- Phospholemman
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit alpha-1
- Mitogen-activated protein kinase 3
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGALLCFLAYGILAAMEDEPSNDNLYLGIVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGQTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILRDHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTTNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
Protein: Bmal2 (Q9IAU1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDNLEMKSASNLDEDMEDDAGRSEDDQHLKIKCIREPHSQIEKRRRDKMNNLIDELAAMIPTCNPMSRKLDKLTVLRMAVQHLKSLKGATSSFAEANYKPAFLPDDELKHLVLRAADGFLFVVGCDRGKIVFVSESVSKTLNYSRTELIGQSLFDYVHPKDIGKVKEQLSASELYPRERLIDAKTGLQVQAELPVGSARLCSGARRSFFCRMKYNKITVKEEKDFQAGASKKKESQRYCTVHCTGYMRTWPTRQLATEGEAEADKESSHFSCLVAMGRVHPHTLPQANGEIKVKPTEFVTRYAMDGKFTFVDQRATTILGYLPQELLGTSCYEYFHLDDLPHLAERHRKVLRSKEKIETNCYKFKTKSGSFVNLQSQWFSFINPWTKEVEYIVSTNTVVSGKSNPGGSGDKAEQPSSSKASEDDAKKSQQVPIIPGISSASGMIYAGCIGTQIANEIMDFNRMNSSPSSGNTSPFSLLQDKSPLALAQASSNVPNGEATDVEMPGKSSSEEEARGGPFSTGDNLMEASSQLDLEGVPGLGALSTDEAAMAVIMSLLETDANLGEAVNFDEMHWSL
Protein: Peptidase C13 family (Putative GPI-anchor transamidase) (Q8GYI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- GPI transamidase subunit PIG-U
- GPI transamidase subunit PIG-U
- GPI transamidase component Gpi16 subunit family protein
- GPI transamidase component PIG-S-like protein
- GPI transamidase component family protein / Gaa1-like family protein
- GPI inositol-deacylase
- Uncharacterized protein
- GPI ethanolamine phosphate transferase 3
- At1g16040
- Mannosyltransferase APTG1
Sequence:
MKILTLVMLLCYSFVSSTGDTTIHTNNWAVLVCTSRFWFNYRHMANTLSLYRTVKRLGIPDERIILMLADDMACNARNEYPAQVFNNENHKLNLYGDNVEVDYRGYEVTVENFLRVLTGRHENAVPRSKRLLSDEGSHILLYMTGHGGDEFLKFQDAEELQSHDLADAVKQMKEKRRFKELMIMVDTCQAATLFNQLQSPGVLAIGSSLKGENSYSHHLDSDIGVSVVDRFTYYTLAFFERLNIYDNASLNSLFRSYDPRLLMSTAYYRTDLYQPHLVEVPVTNFFGSVMETIHTDSAYKAFSSKISERKINSEMPFNQLSEHDLKEELENTNIPNDELIAEKQKCPYSQMRADLHEKVEKLENVDTVVNLSIAVMVLAVMVSSSLLR
Protein: Uncharacterized protein (Q580S6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Intraflagellar transport protein component, putative
- Intraflagellar transport protein IFT88, putative
- Intraflagellar transport protein 80
- Intraflagellar transport protein 56 homolog
- IFT80/172/WDR35 TPR domain-containing protein
- Intraflagellar transport protein A1
- C2H2-type domain-containing protein
- Intraflagellar transport protein 57/55
- Ankyrin repeat protein
- Intraflagellar transport complex B protein 46 C terminal
Sequence:
MGVAGGLVTAGMRPTTTSGGGTTLGRIQAKIQDGNFTATVYGYIRDHKYDEAIEVLLLQLDEFPRSRAAISLIAYCYYHVGDFAEAARMYQQLVKICPNVEEYRVYLCQSLYKAGAYVEASKMCTMIESEQYSMRLMKLQASIAYEQEEIPQTKSFLEKCPPEDPEVIILQGCVLCNEGSYEEALAKFQEAQAGLGFKPDLAYNIALTYYRMQQYGPSLKHIAEIIERGIQEHPELNIGSNTEGNEARSVGNTQLLKETALVEAFNLKTAIEFMMKNMSAAKEALTDMPPRLQEELDPVTLHNTALVNMPEDPSIGFSKLNFLLQNPPFPPETFQNLLLFYCKYQYFDLAADVLAENPHLSWKYLSQQNQSLYDFLDGLITAQTSPAEAYRKFDILAQHHIDQLRRLTKKLQDAKQNQDKNSVRTALRNYDEALEDYIPVLMAQANIYWEIENYPMVEKLFRQSAEFCSEHEIWKLNVAHVFFMQETKFREAIRYYEPVVEANEENLLNCSAIVLANLCVAYIMTALNDKAEEIMRRIEREEEKLLYVDPEKQPLHLCIVNLVIGTLYCSKGNFEFGISRIVKSLEPYHRKIMTDTWFYAKRCFLALAMHLAKHMVVLKDGTFDEILNFFDQADRYGEKIPAFVHPDPSKQENTSKNTVRWEARQLKHLYLHMRE
Protein: Imidazole glycerol phosphate synthase hisHF (IGP synthase) (IGPS) (ImGP synthase) (EC 4.3.2.10) [Includes: Glutaminase (EC 3.5.1.2); Cyclase] (P33734)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain.
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase
- Histidine biosynthesis trifunctional protein
- 1-
- ATP phosphoribosyltransferase
- Histidinol-phosphate aminotransferase
- Bifunctional purine biosynthetic protein ADE5,7
- Adenylyl cyclase-associated protein
- Bifunctional purine biosynthesis protein ADE17
- Bifunctional purine biosynthesis protein ADE16
- DNA repair protein RAD16
Sequence:
MPVVHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDFNISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGICVGLQALFAGSVESPKSTGLNYIDFKLSRFDDSEKPVPEIGWNSCIPSENLFFGLDPYKRYYFVHSFAAILNSEKKKNLENDGWKIAKAKYGSEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLKQQSPPIPNYSAEEKELLMNDYSNYGLTRRIIACLDVRTNDQGDLVVTKGDQYDVREKSDGKGVRNLGKPVQLAQKYYQQGADEVTFLNITSFRDCPLKDTPMLEVLKQAAKTVFVPLTVGGGIKDIVDVDGTKIPALEVASLYFRSGADKVSIGTDAVYAAEKYYELGNRGDGTSPIETISKAYGAQAVVISVDPKRVYVNSQADTKNKVFETEYPGPNGEKYCWYQCTIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDGSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTRADACLGAGMFHRGEFTVNDVKEYLLEHGLKVRMDEE
Protein: Protein CBP3, mitochondrial (P21560)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Chaperone required for the assembly of ubiquinol-cytochrome c reductase of the mitochondrial respiratory chain.
Subcellular location: Mitochondrion membrane.
Interaction partners:
- Assembly factor CBP4
- Cytochrome B pre-mRNA-processing protein 6
- Cytochrome b
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Mitochondrial chaperone BCS1
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
Sequence:
MMSVNRFTSGRLPVFLRKSPFYYSRAYLHQTCVFKQNKETAQDSPELLAKSSHLNSKPLDVSNKAPVKTAQNKIPLAHSKYESSKYELPKWKEALGELVIRAFHLDMDRVRAGPVAGSYYYKICKEQGLQYEDEPLSETAKYFYEDLKLPRTFSQWFQITVLHEWILFVRMRAMPFKYGRNYQQKLVDRTFSDIELRLFEEMKVNSGRIADQYLKDFNTQLRGAIFAYDEGFATDDGTLATAVWRNLFGGRKNIDMVHLESVVRYIYSQLYVLSRLSDREFATGKFKFVPPGVKVEKLTPKQEEELKAKTIAKYEALDKDPKTLPSERSRLSYTN
Protein: Cystatin fetuin-B-type domain-containing protein (A0A060Y5T9)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Uncharacterized protein
- AAA+ ATPase domain-containing protein
- Metalloendopeptidase
- EGF-like domain-containing protein
- Metalloendopeptidase
- Metalloendopeptidase
- MAM domain-containing protein
- MATH domain-containing protein
- Uncharacterized protein
- Protein unc-79 homolog
Sequence:
MKQCALLLLACVYAHAAPLEAGMKPGSCQDAALDKINKDRTEGYVFGLHRLSNVNQMEHGETGVVFYLTMDVLETDCHVVSKKNAKDCEVPKAENTPVYGQCKAVIYMNRVHRVVRLYNYNCVVRPAAAAKVAKQCPDCPSAMPKDHPEILKTATLSMEKFNKDSGLANHFAILNITRARTSMGMATFYFAEFTIQETTCANTTDPSAASKCPLMACEFAHKGHCKGSHSHDMGGQEFVTVNCEVFENENSKKEKAAHLLGGETDHSHTLQSGKHGKDHTHNASGAHDHAHDHAHDHTKDHKHDGAHAHDHKDGAHGHSHGDGAAGGHDHSHDHGHGHDHAHAHHAKAHNHSTDTGPHQHHNYKHDGEGHTHEHDHELSLDHDHKHAHLHEHEHHHHHHEHPHGTESRHPPQGTVTVLPALGLPMTLPSFPEQPVGEKGAILPMVQDPKIPGMSQPTILPFPTTVSAQCPAEVKDEDNFLFAEDPLFKAAA