wanglab/gogpt-training-data huggingface dataset:
Protein: Exosome complex exonuclease RRP40 (Q38EN5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Exosome component CSL4
- Ribosomal RNA-processing protein 43
- Ribosomal RNA processing protein 4
- Ribosomal RNA processing protein 45
- ATP-dependent DEAD/H RNA helicase, putative
- Elongation factor 1-alpha, putative
- Ribosomal RNA processing protein 6
- Exosome complex exonuclease RRP41A
- Exosome-associated protein 4
Sequence:
MSETNPVVRGAVGVHELAPLCSHVCLPGESVLLLEPTAVVTLGSGLHPLQQDGSDDRKESFEASGEEGSTVVVSEFCGPVLRTAGPNHTQLYKLNGPAARRYMYAARDPVVAIVMKKNASYYSCYTGAASLAVLDALGFDGATKTNKPRLQEGDVVYAFVKGNADASSLDTKFDDGRVVVSSSDEVELSCMAAEVGLVARDWTSAEAVFGPLVGGTVVRVALPYARSLIDGPASRLLALLGDRVPYDVCVGVNGLVWVRGHPSAADPTAAARRTVAVAACVVEAQDAATLEEMEAHVRGYFPKE
Protein: P-loop containing nucleoside triphosphate hydrolases superfamily protein (F4IXH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKSSHEVTKNHSGSPSGKKSKKLAAICEEEYKKNHGESQDRDGGSGLACADSELRRSSRVRKIPSILDASPPPPKKRQRFNKSSSSIEKGKRNEDGDSDAPDGWKSRLRSRRKKNVGFQASGRQRRVVKGKRKLVFRNRACELSEKAEASDREEEKGALKGGKLNKAKKPVDVKESESSEDGGKESDTSNSEDVQKESDTSNSEDESASESEESMQADSAAREKYQEKKATKRSVFLESENEAEVDRTETESEDGTDSTDNEIDDSDEEGESETQCSAEKTGSETEANVEEMRADTNVTMEAVQNESRNQMEELENEIEMGVEDEKKEMSVIVSESGNGTGIREDENKEMDVIVSESGNGTGILEGENKKMEVMVSGSGNGTGIREDDSDFAAKVKNREGDTLHPELLGEASTEINESLKQNDDIGEQGVSRTPSNNKTKEHNEFLDRGGESVEMPDELPIQNETCKKAVDSVSTSSDRLGKPLFKQTRRCGLCGVGTDGKLPKKLMQDNGDSDVEAPSGSSSSEEQKYDILDGFGDDPGWLGRLLGPINDRYGISGTWVHQNCAVWSPEVYFAGVGCLKNIRAALFRGRSLKCTRCDRPGATTGCRPCARANGCIFDHRKFLIACTDHRHHFQPHGRQCQVRMTKMKTKRMRLEMKKHSNDAWRKDVEAEEKWFEKCGEDEEFLKRESKRLHRDLLRVAPEYIGGSDSESGKAFEGWDSVAGLEGVTQCMKEVVLIPLLYPEFFDNLGLTPPRGILLHGHPGTGKTLVVRALIGSLARGNRRIAYFARKGADCLGKYVGDAERQLRLLFQVAEKCQPSIIFFDEIDGLAPKRSRQQDQTHSSVVSTLLALLDGLKSRGSVVVIGATNYPDAIDPALRRPGRFDREIYFPLPSVDDRAAIISLHTRKWPKPVSGYLLKWIAKETAGFAGADIQALCTQAAMIALNRSFPLQESLAAAELGVSSSNRAALPSFSVEERDWLEALSRSPPPCSRRGAGIAASDIFSSPLPTYLVPSLLPPLCSLLVALHLDERIFLPPLLSKAAVDVQNVIRSALSDKKITEGCWWSHVDTLLHEVDVVKDIVQRLSCTGILDGGCDLVGSVASIPGTGDCSLGSAKFMVPRVCRHPGVLGNASVESTSKSGFQLLIAGGPKSGQRHLASCVLHCFIGNAEMLKIDTATISQEGNGDLVLGVTHLLIKCASKKSCVVFMPRVDLWAVKTETPLNEEVECDDDSVQENCSEMGEEKALQNGVRVSHAWNTFFEQVETLRVSTKMMILATSGMPYKLLPPKIQQFFKTDLSKECQPTMSEAVPQFNVQVVESSDQDIAIDLSATELLRRAIQVFLHLVHQGSHTHCGLKKKYKGEDLDQGCRDAAPQNNTDHRAGEEAVVKSKRLDDGSLKVPPLPININVKPKSSLQLAVSTFGYQILQYPQFAELCWVTSKLKEGPSADVSGPWRGWPFNSCITRPCNSSEQTITSSDSNNVKGKDSTGIVRGLTAVGLSAYRGTYISLREVSFEVRKVLELLVGRISVKINAGKDRCRYIRILSQVAYLEDLVNSWVYAMRSFESTTQTESTNPLPCSVVNPSVRNEPTEQGTSDQLKGSEEDLKEDTQNMNCPDPIASSNLTDNHQPVVEIANGHNGTNHESFLEDTGHLTTHSTDGLTLVKENVDVISDTEMMIEDSGVNPFRQAVLLDLNSPAADHEQNETPHGSCEVETTGTVISLQEKADSLDNPNGSGDSNSISLEDPHKSADSNNGKAWDGVHGLESANNMPEPVEQVETTGRTNPQDDPSLVCLYRCCSQCVSILQDSMHKLVTRELRLGRSSITTEGIHDAVSSLSVELISAVRKFISVKNNGTMQEAKVKDHEECPENEACFCKRLSGNFLASVECCSHSAEMQGSLDEGNTYRRPKTWLEPVFVFKDGILVPVSTEDDRSLHCKYDSFCLGSLIELIATEMKPF
Protein: Polyamine aminopropyltransferase (Agmatine aminopropyltransferase) (EC 2.5.1.104) (Cadaverine aminopropyltransferase) (EC 2.5.1.-) (N1-aminopropylagmatine synthase) (Putrescine aminopropyltransferase) (PAPT) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16) (Q5JFG9)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1-aminopropylagmatine. It can also use cadaverine (1,5-diaminopentane) and putrescine (1,4-diaminobutane) as substrate with a lower activity than that of agmatine. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:20675472}.
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme
- N
- Arginase
- Arginase
- S-methyl-5'-thioadenosine phosphorylase
- Probable 6-oxopurine nucleoside phosphorylase
- 5-methylthioadenosine/S-adenosylhomocysteine deaminase
- Hypothetical membrane protein, conserved
- Pyruvoyl-dependent arginine decarboxylase
- Hypothetical membrane protein, conserved
Sequence:
MGYNEQERAFIEWYPRGYGVGFKVKRRLFETQTEYQRLEIYETEGFGKLLVLDGTVQLVEVGEESYHEVLVHPVMLAHPNPRKVLVIGGGDGGTLREVLRHDTVEKAIMVEIDEGVVEASYLYLDVAKDLLDRLIKKEEPRAELIIGDGVKYLRETDERFDVIIVDSTDPVGPAKLLFSEEFYRDAYEKLNEKGLYVTQAGSVYLFTNELLDAYKAMKKVFDRVYYFSFPVIGYASPWSFLVGVKGDVDFTRIDLERAKKLDLYYYDPERHETLFQMPRYVRKLLEGQ
Protein: Keratin, type I cytoskeletal 40 (Cytokeratin-40) (CK-40) (Keratin-40) (K40) (Type I hair keratin Ka36) (Q6A162)
Organism: Homo sapiens (Human)
Function: May play a role in late hair differentiation.
Interaction partners:
Sequence:
MTSDCSSTHCSPESCGTASGCAPASSCSVETACLPGTCATSRCQTPSFLSRSRGLTGCLLPCYFTGSCNSPCLVGNCAWCEDGVFTSNEKETMQFLNDRLASYLEKVRSLEETNAELESRIQEQCEQDIPMVCPDYQRYFNTIEDLQQKILCTKAENSRLAVQLDNCKLATDDFKSKYESELSLRQLLEADISSLHGILEELTLCKSDLEAHVESLKEDLLCLKKNHEEEVNLLREQLGDRLSVELDTAPTLDLNRVLDEMRCQCETVLANNRREAEEWLAVQTEELNQQQLSSAEQLQGCQMEILELKRTASALEIELQAQQSLTESLECTVAETEAQYSSQLAQIQCLIDNLENQLAEIRCDLERQNQEYQVLLDVKARLEGEINTYWGLLDSEDSRLSCSPCSTTCTSSNTCEPCSAYVICTVENCCL
Protein: Glutinol synthase (KdGLS) (EC 5.4.99.49) (E2IUA7)
Organism: Kalanchoe daigremontiana (Devil's backbone) (Bryophyllum daigremontianum)
Function: Oxidosqualene cyclase that generates glutinol, a triterpenoid product. Glutinol is probably required to coat the leaf exterior as a defense compound against pathogens or herbivores.
Interaction partners:
Sequence:
MWKLKIADGGSNPYIFTTNNFVGRQIWEFDPQATDPQQLAKVEAARLDFYHNRYKLKPNSDLLWRMQFLEEKDFRQNIPQVKVEDGEEVSYEAVTAALRRGVHLYSALQASDGHWPAENAGPMFFMPPMVMCLYITGHLNAIFTEEHRSETLRYIYYHQNEDGGWGFHIEGHSTMFGTVLNYICMRLLGEGPEGGQDNAVSRGRKWILDHGGATSIPSWGKTWLSIMGLCDWSGCNPMPPEFWLLPSYLPMHPGKMWCYCRMVYMPMSYLYGKRFTARITPLILQLREEIHIQPYDQIDWKKVRHVCCKEDMYYPHPLLQDLLWDTLYLTTEPLLTRWPLNKLIRQRALQKTMKHIHYEDENSRYITIGTVEKVLCMLACWVEDPNGDYFKKHLARVPDYFWVAEDGMKIQSFGSQHWDTVFSAQALLASDMADEIGTTLAKAHYCIKESQVKDNPSGDFRSMYRHISKGSWTFSDQDHGWQLSDCTAEGLKCCLLFSLMQPEVVGEAMPPERLFDSVNILLYLQSKNGGMPGWEPAGASEWLELLNPTEFFENIVIEHEYVECTSSAVQALVLFKKLHPGHRRKEVERFITNGAKYIEDIQMPDGAWYGNWGVCFTYGAWFALGGLAAAGKTYNNCAAVRKGVDFLLRIQLEDGGWGESYQSCPDKKYVPLEDNRSNLVHTSWALMGLLCSGQADRDPNPLHRAAKLLINSQLEDGDFPQQEITGVFKMNCMLHFAAYRSIFPVWALAEYKRFCNLSSEAISKPSK
Protein: Uncharacterized protein (Q386U3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQSRRNSMMNRVCRKYARVPGQHGDGNVPAFYPIAINPGWWGQPFGKVKDAKGQILFFYGLVLPIALYWIFDVTFAQRTRVGNVGKRPMYSNFFFRQMDLDDPDHAIKYEKLRQEIAENKLEVRWGGTNFLASYLWEPGDPEPDIRRREVHAHH
Protein: Major prion protein (PrP) (CD antigen CD230) (P13852)
Organism: Rattus norvegicus (Rat)
Function: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000250|UniProtKB:P04156}.
Interaction partners:
- Neural cell adhesion molecule 1
- Stress-induced-phosphoprotein 1
- Amyloid-beta precursor protein
- Tyrosine-protein kinase Fyn
- Neural cell adhesion molecule 2
- Ig-like domain-containing protein
- Caveolin-1
- Alpha-synuclein
- Endoplasmic reticulum chaperone BiP
- Glycogen synthase kinase-3 beta
Sequence:
MANLGYWLLALFVTTCTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQSGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWSQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMLHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSAVLFSSPPVILLISFLIFLIVG
Protein: Heat shock protein SSA1 (Heat shock protein YG100) (P10591)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Secreted, cell wall {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mitochondrial protein import protein MAS5
- ATP-dependent molecular chaperone HSP82
- ATP-dependent molecular chaperone HSC82
- Protein SIS1
- Heat shock protein 104
- Heat shock protein STI1
- Heat shock protein homolog SSE1
- Heat shock protein SSA2
- Eukaryotic peptide chain release factor GTP-binding subunit
- Heat shock transcription factor
Sequence:
MSKAVGIDLGTTYSCVAHFANDRVDIIANDQGNRTTPSFVAFTDTERLIGDAAKNQAAMNPSNTVFDAKRLIGRNFNDPEVQADMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTKKSEIFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADKDTVTKKAEETISWLDSNTTASKEEFDDKLKELQDIANPIMSKLYQAGGAPGGAAGGAPGGFPGGAPPAPEAEGPTVEEVD
Protein: IAA-amino acid hydrolase ILR1-like 4 (EC 3.5.1.-) (jasmonoyl-L-amino acid hydrolase) (EC 3.5.1.127) (O04373)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA), including IAA-Ala, IAA-Asn, IAA-Cys, IAA-Glu, IAA-Met, IAA-Ser and IAA-Gly. Has a lower efficiency with IAA-Phe, IAA-Leu and IAA-Val and no activity with IAA-Ile. Important for IAA-Leu hydrolysis in roots. Also hydrolyzes amino acid conjugates of jasmonic acid and 12-hydroxy jasmonic acid.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Protein LONG AFTER FAR-RED 3
- Cytochrome P450 94C1
- Cytochrome P450 94B3
- Cytochrome P450 94B1
- Auxin response factor 6
- Cytosolic sulfotransferase 15
- Amidase 1
Sequence:
MSFFKWVSFVLILHLLNPTLISCSSNGLSQIPSKFLTLAKRNDFFDWMVGIRRRIHENPELGYEEVETSKLVRAELEKMGVSYKYPVAVTGVVGYVGTGHAPFVALRADMDALAMQEMVEWEHKSKVPGKMHACGHDAHTTMLLGAAKLLKEHEEELQGTVVLVFQPAEEGGGGAKKIVEAGVLENVSAIFGLHVTNQLALGQVSSREGPMLAGSGFFKAKISGKGGHAALPQHTIDPILAASNVIVSLQHLVSREADPLDSQVVTVAKFEGGGAFNVIPDSVTIGGTFRAFSTKSFMQLKKRIEQVITRQASVNMCNATVDFIEEEKPFFPPTVNDKALHQFFKNVSGDMLGIENYVEMQPLMGSEDFSFYQQAIPGHFSFVGMQNKARSPMASPHSPYFEVNEELLPYGASLHASMATRYLLELKASTLNKSNKKDEL
Protein: Protein MAK16 homolog (Q57WF3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RNA processing factor 1, putative
- Uncharacterized protein
- Ribosome biogenesis protein NSA1
- 60S ribosomal protein L24, putative
- rRNA processing protein, putative
- Ribosome biogenesis protein, putative
- CCAAT-binding factor domain-containing protein
- RNA-binding protein, putative
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein NSA2 homolog
Sequence:
MNHDDAMWNVMGQTFCSFKVKTHDDKARFCRNPYNVTGLCQRGVCPLSNAQYATVVEHDDELYLYVKTAERAHLPRRQWEKVRLDANFPRALAQIDEELQWWDQKLVNKVKARLLRLKQYLMRRRKMLLEPKVEYVSVNKRQEDKLIRREAKAEAAARLELEVEKELLERLRSGTYDSVINCSLEAFERVLDREEDRTEFEALEDEEDEEFPEFVMDDELDEEEEMEESNRKIGKRGDSSVVHRSGRGTRRQRLVIEEEVEQEPVSKRVRTADLDW
Protein: Condensin-2 complex subunit H2 (Chromosome-associated protein H2) (hCAP-H2) (Kleisin-beta) (Non-SMC condensin II complex subunit H2) (Q6IBW4)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture. May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Required for decatenation of chromatin bridges at anaphase. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (By similarity). Seems to have lineage-specific role in T-cell development.
Subcellular location: Nucleus {ECO:0000269|PubMed:14532007}. Chromosome {ECO:0000269|PubMed:14532007}. Note=Distributed along the arms of chromosomes assembled in vivo and in vitro.
Interaction partners:
- Structural maintenance of chromosomes protein 4
- Condensin-2 complex subunit D3
- Condensin-2 complex subunit G2
- Structural maintenance of chromosomes protein 2
- Condensin complex subunit 1
- Condensin complex subunit 2
- Condensin complex subunit 3
- Lysophospholipid acyltransferase 5
- Telomeric repeat-binding factor 1
Sequence:
MEDVEARFAHLLQPIRDLTKNWEVDVAAQLGEYLEELDQICISFDEGKTTMNFIEAALLIQGSACVYSKKVEYLYSLVYQALDFISGKRRAKQLSSVQEDRANGVASSGVPQEAENEFLSLDDFPDSRTNVDLKNDQTPSEVLIIPLLPMALVAPDEMEKNNNPLYSRQGEVLASRKDFRMNTCVPHPRGAFMLEPEGMSPMEPAGVSPMPGTQKDTGRTEEQPMEVSVCRSPVPALGFSQEPGPSPEGPMPLGGGEDEDAEEAVELPEASAPKAALEPKESRSPQQSAALPRRYMLREREGAPEPASCVKETPDPWQSLDPFDSLESKPFKKGRPYSVPPCVEEALGQKRKRKGAAKLQDFHQWYLAAYADHADSRRLRRKGPSFADMEVLYWTHVKEQLETLRKLQRREVAEQWLRPAEEDHLEDSLEDLGAADDFLEPEEYMEPEGADPREAADLDAVPMSLSYEELVRRNVELFIATSQKFVQETELSQRIRDWEDTVQPLLQEQEQHVPFDIHTYGDQLVSRFPQLNEWCPFAELVAGQPAFEVCRSMLASLQLANDYTVEITQQPGLEMAVDTMSLRLLTHQRAHKRFQTYAAPSMAQP
Protein: SD27884p (Q8MRT0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLAQKSVAGADELAQAKGKCVHCANAAERVCQRCGDFYCSKHCQRQDWLRHRYICIPLPALVSPNEYSVFQSDRESTLEGACSLNADKSVVEASPIPLSRSPILPDLQCNNAGRSSIIAAKDDIPVSPPKAIIPPSGAMVYITDFISSNRCYIRDASESAERAFDEVCKKVNTIATLLPRIKNPPPNRLCLVHFNGMYVRAKMCKKLREVSHLFLVDLGIKHSGPFFDFKDINDELKALPCSSQLVQLKNVLNCDYSNDVIAFNSKFVGKKYMATIKKCPGLHLVELVNTEMNFSVNEQLNAFFNSKKLLRNPNSAAENIKSCSLEGPQPSHIDQPIAIPAIECKKMLTKPEVQNECEEILKQQNSGQIDQSKSTNVLVTEGASNKMLGFIDLADKATKTDQDTAPKPKDEDVKHSLTQCLTPKANYPLQLPNHKKNLELPVIHKTNAQTNGIVMSKNEHVLKPVS
Protein: Interferon alpha-inducible protein 27-like protein 2A (Interferon-stimulated gene 12 protein) (ISG12) (Q8R412)
Organism: Mus musculus (Mouse)
Function: May be involved in the interferon-induced negative regulation of the transcriptional activity of NR4A1, NR4A2 and NR4A3 through the enhancement of XPO1-mediated nuclear export of these nuclear receptors. Through the regulation of NR4A1 transcriptional activity, may play a role in the vascular response to injury.
Subcellular location: Nucleus inner membrane {ECO:0000305|PubMed:22427340}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ubl carboxyl-terminal hydrolase 18
- Receptor-transporting protein 4
- Ubiquitin-like protein ISG15
- Interferon-induced protein 44
- Antiviral innate immune response effector IFIT1
- Interferon-induced protein with tetratricopeptide repeats 3
Sequence:
MLGTLFGSAIGGALAVAGAPVALAAMGFTGTGIAAASIAAKMMSAAAIANGGGVAAGSLVATLQSAGVLGLSTSTNAILGAAGAAVGALL
Protein: Uncharacterized protein YMR074C (Q04773)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YOL098C
- Uncharacterized protein YEL057C
- Elongation factor 1-beta
- Zinc finger protein YPR022C
- Small ribosomal subunit protein uS3
- Prefoldin subunit 4
- Prefoldin subunit 1
- T-complex protein 1 subunit alpha
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL30m
Sequence:
MDPELQAIREARLAQLKNNSGGTNGDRNSGANNGGGENSAPVGAAIANFLEPQALERLSRVALVRRDRAQAVETYLKKLIATNNVTHKITEAEIVSILNGIAKQQNSQNNSKIIFERKDFSEDLNSFDKQNAKNDDDEDDDDFFD
Protein: N-ethylmaleimide reductase (NEM reductase) (EC 1.3.1.-) (N-ethylmaleimide reducing enzyme) (P77258)
Organism: Escherichia coli (strain K12)
Function: Involved in the degradation of toxic compounds. Can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones. Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. Catalyzes the reduction of N-ethylmaleimide (NEM) to N-ethylsuccinimide. Together with NfsA and NfsB, can use the nitroaromatic explosive 2,4,6-trinitrotoluene (TNT).
Interaction partners:
- HTH-type transcriptional repressor NemR
- Lactoylglutathione lyase
- Oxygen-insensitive NAD
- Oxygen-insensitive NADPH nitroreductase
Sequence:
MSSEKLYSPLKVGAITAANRIFMAPLTRLRSIEPGDIPTPLMAEYYRQRASAGLIISEATQISAQAKGYAGAPGIHSPEQIAAWKKITAGVHAENGHMAVQLWHTGRISHASLQPGGQAPVAPSALSAGTRTSLRDENGQAIRVETSMPRALELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNHRTDQYGGSVENRARLVLEVVDAGIEEWGADRIGIRVSPIGTFQNTDNGPNEEADALYLIEQLGKRGIAYLHMSEPDWAGGEPYTDAFREKVRARFHGPIIGAGAYTVEKAETLIGKGLIDAVAFGRDWIANPDLVARLQRKAELNPQRAESFYGGGAEGYTDYPTL
Protein: Serine/threonine-protein kinase plo1 (EC 2.7.11.21) (Polo kinase plo1) (P50528)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required to form a bipolar spindle, the actin ring and septum. Functions upstream of the whole septum formation pathway, including actin ring formation (regulated by late septation genes) and septal material deposition (regulated by early septation genes). Behaves as a 'septum-promoting factor', and could also be involved in inducing other late events of cell division. Together with moa1, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage.
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:25533956}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:11676915, ECO:0000269|PubMed:12615979, ECO:0000269|PubMed:12815070, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cell division control protein 16
- Tyrosine-protein phosphatase CDC14 homolog
- M-phase inducer phosphatase
- Septum-promoting GTP-binding protein 1
- Separin
- Serine/threonine-protein kinase cds1
- Mitosis inhibitor protein kinase wee1
- Cohesin subunit rad21
- Meiotic recombination protein rec8
- Structural maintenance of chromosomes protein 1
Sequence:
MASVAIKEPKTAITPKKKSKASRLCFTPPTNLHNNKKNIFYTRYDCIGEGGFARCFRVKDNYGNIYAAKVIAKRSLQNDKTKLKLFGEIKVHQSMSHPNIVGFIDCFEDSTNIYLILELCEHKSLMELLRKRKQLTEPEVRYLMMQILGALKYMHKKRVIHRDLKLGNIMLDESNNVKIGDFGLAALLMDDEERKMTICGTPNYIAPEILFNSKEGHSFEVDLWSAGVVMYALLIGKPPFQDKEVKTIYRKIKANSYSFPSNVDISAEAKDLISSLLTHDPSIRPSIDDIVDHEFFHTGYMASTLPDEILHSMPIWPSSQSKSSFQRNLDFVASASGVGFGNSAGVEKNKPYALRTDEVDNDRILPSVLSPRDRVNPVMKIGPETKPVPSKLSTALHAARKSTDGSLGSRVKVLREESQSFVPTKSAVTEQVEPIQLIRSLSANTVSRLSKVGNMKSDIWISVKKTALKIGMALEAHTHALTSEDADSEPVLFITKWVDYSNKYGLGYQLSDESVGVHFNDDTSLLFSADEEVVEYALHPKDTEIKPYIYPASKVPESIRSKLQLLKHFKSYMGQNLSKAVQDESFEKPKNSTSNTMLFMQHYLRTRQAIMFRLSNGIFQFNFLDHRKVVISSTARKIIVLDKERERVELPLQEASAFSEDLRSRLKYIRETLESWASKMEVS
Protein: Lutropin subunit beta (Lutropin beta chain) (Luteinizing hormone subunit beta) (LH-B) (LSH-B) (LSH-beta) (P45657)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Function: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MGGAQVLLLLTLLGTPLVTHGTPPLVVDPSIGSQLGLGSVLGLDLGSMGGSGRPPCRPINVTVAVEKEECPQCMAVTTTACGGYCRTREPVYRSPLGPPPQSSCTYGALRYERWDLWGCPIGSDPKVILPVALSCRCARCPIATSDCTVQGLGPAFCGAPGGFGGQ
Protein: Calmodulin, putative (C4M0U8)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Interaction partners:
- Calcium binding protein 2
- Calcium binding family protein
- Calmodulin, putative
- Calmodulin, putative
- Calmodulin, putative
- Calmodulin, putative
- AP-1 complex subunit gamma
- Myosin heavy chain
- Actin, putative
- Actin, putative
Sequence:
MSEQKKVLTAEEQQEYKEAFQLFDKDNDNKLTAEELGTVMRALGANPTKQKISEIVKDYDKDNSGKFDQETFLTIMLEYGQEVDSTEDIKKAFEIFDKEKNGYISASELKHVLTTLGEKLTEQEVDDLLKEIGVEEGLINVDDFVKLITSK
Protein: Perilipin 4 (A0A0J9YXN7)
Organism: Homo sapiens (Human)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
MSAPDEGRRDPPKPKGKTLGSFFGSLPGFSSARNLVANAHSSARARPAADPTGAPAAEAAQPQAQVAAHPEQTAPWTEKELQPSEKQMVSGAKDLVCSKMSRAKDAVSSGVASVVDVAKGVVQGGLDTTRSALTGTKEVVSSGVTGAMDMAKGAVQGGLDTSKAVLTGTKDTVSTGLTGAVNVAKGTVQAGVDTTKTVLTGTKDTVTTGVMGAVNLAKGTVQTGVETSKAVLTGTKDAVSTGLTGAVNVARGSIQTGVDTSKTVLTGTKDTVCSGVTGAMNVAKGTIQTGVDTSKTVLTGTKDTVCSGVTGAMNVAKGTIQTGVDTSKTVLTGTKDTVCSGVTGAMNVAKGTIQTGVDTTKTVLTGTKNTVCSGVTGAVNLAKEAIQGGLDTTKSMVMGTKDTMSTGLTGAANVAKGAMQTGLNTTQNIATGTKDTVCSGVTGAMNLARGTIQTGVDTTKIVLTGTKDTVCSGVTGAANVAKGAVQGGLDTTKSVLTGTKDAVSTGLTGAVNVAKGTVQTGVDTTKTVLTGTKDTVCSGVTSAVNVAKGAVQGGLDTTKSVVIGTKDTMSTGLTGAANVAKGAVQTGVDTAKTVLTGTKDTVTTGLVGAVNVAKGTVQTGMDTTKTVLTGTKDTIYSGVTSAVNVAKGAVQTGLKTTQNIATGTKNTFGSGVTSAVNVAKGAAQTGVDTAKTVLTGTKDTVTTGLMGAVNVAKGTVQTSVDTTKTVLTGTKDTVCSGVTGAANVAKGAIQGGLDTTKSVLTGTKDAVSTGLTGAVKLAKGTVQTGMDTTKTVLTGTKDAVCSGVTGAANVAKGAVQMGVDTAKTVLTGTKDTVCSGVTGAANVAKGAVQTGLKTTQNIATGTKNTLGSGVTGAAKVAKGAVQGGLDTTKSVLTGTKDAVSTGLTGAVNLAKGTVQTGVDTSKTVLTGTKDTVCSGVTGAVNVAKGTVQTGVDTAKTVLSGAKDAVTTGVTGAVNVAKGTVQTGVDASKAVLMGTKDTVFSGVTGAMSMAKGAVQGGLDTTKTVLTGTKDAVSAGLMGSGNVATGATHTGLSTFQNWLPSTPATSWGGLTSSRTTDNGGEQTALSPQEAPFSGISTPPDVLSVGPEPAWEAAATTKGLATDVATFTQGAAPGREDTGLLATTHGPEEAPRLAMLQNELEGLGDIFHPMNAEEQAQLAASQPGPKVLSAEQGSYFVRLGDLGPSFRQRAFEHAVSHLQHGQFQARDTLAQLQDCFRLIEKAQQAPEGQPRLDQGSGASAEDAAVQEERDAGVLSRVCGLLRQLHTAYSGLVSSLQGLPAELQQPVGRARHSLCELYGIVASAGSVEELPAERLVQSREGVHQAWQGLEQLLEGLQHNPPLSWLVGPFALPAGGQ
Protein: Sphingolipid delta(4)-desaturase DES1-like (EC 1.14.19.17) (Q9ZPH4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sphingolipid-delta-4-desaturase required for the biosynthesis of delta-4-unsaturated sphingolipids and derivatives. May be required for the biosynthesis of glucosylceramides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- 3-dehydrosphinganine reductase TSC10A
- 3-dehydrosphinganine reductase TSC10B
- ceramide glucosyltransferase
- Alkaline ceramidase
- Ceramide kinase
- Sphingosine kinase 2
- Sphingosine kinase 1
- Neutral ceramidase 2
- Neutral ceramidase 3
- Neutral ceramidase 1
Sequence:
MGKGGREKISSNEEEREGVMATDFFWSYTDEPHASRRRQILSCYPQIRQLFGPDPWAFLKITLVVILQLSTAAILHNSGWLKILSIAYFFGSFLNHNLFLAIHELSHNLAFSTPVYNRCLGIFANLPIGVPMSVTFQKYHLEHHRFQGVDGIDMDVPTYTEAHLVTNIFAKTIWVFLQLFFYALRPIFIKPKPPGYWEFINFLIQIVLDVSVVLFFGWRSFAYLILSTFVGGGMHPMAGHFISEHYVFNPNQETYSYYGPLNLLTWSVGYHNEHHDFPRIPGNKLHLVKEIAGEYYEGLESYKSWSQVIYMYIMDTTVGPYSRMKRKLSKSD