wanglab/gogpt-training-data huggingface dataset:
Protein: Non-classical export protein 2 homolog 1 (Functional homolog of NCE102) (P53279)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in membrane organization. Required for the formation of membrane compartments of CAN1 (MCCs), localization of CAN1 at the MCCs and subsequent invagination of the plasma membrane at the MCCs sites. Involved in eisosome organization and might act as a sensor of sphingolipids that regulates plasma membrane function. Involved in a novel pathway of export of proteins that lack a cleavable signal sequence. Non-classical export pathway functions also as an alternative clearance/detoxification pathway to eliminate damaged material, when the basic repair pathway is not sufficient.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Associates with the ergosterol-rich membrane compartment of CAN1 (MCC). Accumulates in membrane domains at eisosomes. {ECO:0000250}.
Interaction partners:
- Uncharacterized plasma membrane protein YNL194C
- Protein SUR7
- SUR7 family protein FMP45
- Uncharacterized vacuolar membrane protein YNR061C
- Serine/threonine-protein kinase PRR2
Sequence:
MLSAADNLVRIINAVFLIISIGLISGLIGTQTKHSSRVNFCMFAAVYGLVTDSLYGFLANFWTSLTYPAILLVLDFLNFIFTFVAATALAVGIRCHSCKNKTYLEQNKIIQGSSSRCHQSQAAVAFFYFSCFLFLIKVTVATMGMMQNGGFGSNTGFSRRRARRQMGIPTISQV
Protein: DNA nucleotidylexotransferase (EC 2.7.7.31) (Terminal addition enzyme) (Terminal deoxynucleotidyltransferase) (Terminal transferase) (P04053)
Organism: Homo sapiens (Human)
Function: Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:16371131}.
Interaction partners:
- Deoxynucleotidyltransferase terminal-interacting protein 1
- Caspase-3
- Immunoglobulin iota chain
- Deoxynucleotidyltransferase terminal-interacting protein 2
- Apoptosis regulator Bcl-2
- B-cell antigen receptor complex-associated protein alpha chain
- Annexin A5
- Peroxidasin homolog
- Probable oxidoreductase PXDNL
- Aminopeptidase N
Sequence:
MDPPRASHLSPRKKRPRQTGALMASSPQDIKFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIECIRAGKPVEMTGKHQLVVRRDYSDSTNPGPPKTPPIAVQKISQYACQRRTTLNNCNQIFTDAFDILAENCEFRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWAFLPDAFVTMTGGFRRGKKMGHDVDFLITSPGSTEDEEQLLQKVMNLWEKKGLLLYYDLVESTFEKLRLPSRKVDALDHFQKCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTKRIFLKAESEEEIFAHLGLDYIEPWERNA
Protein: Endonuclease III (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase) (P0AB83)
Organism: Escherichia coli (strain K12)
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Interaction partners:
- Ion-translocating oxidoreductase complex subunit E
- Exodeoxyribonuclease III
- Ion-translocating oxidoreductase complex subunit G
- Formamidopyrimidine-DNA glycosylase
- Endonuclease 4
- Uracil-DNA glycosylase
- Ion-translocating oxidoreductase complex subunit D
- Endonuclease 8
- Ion-translocating oxidoreductase complex subunit B
- Ion-translocating oxidoreductase complex subunit C
Sequence:
MNKAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI
Protein: pyridoxal kinase (EC 2.7.1.35) (D6XI07)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pyridoxal phosphate homeostasis protein
Sequence:
MSEKTVLSIQSFVTHGYVGNKAATFPLQLHGFDVDGINTVCLSNHSGYPVIRGHRMSLQEYDELMEGVRANNFLSNYRYILTGYINNVDIIGRIRDTLKEVRELREKEDKKLTFICDPVMGDDGIMYCKKEVLDAYRELVPLADIVTPNYFEASLLSGVTVNDLSSAILAADWFHNCGVAHVIIKSFREQENPTHLRFLYSVKEGSEAAVRRFSGVVPYHEGRYTGTGDVFAACLLAFSHSHPMDVAIGKSMAVLQELIIATRKEGGDGKSSLKSRELRVVASPQVVLQPSTVVDVKPIS
Protein: Exosome complex component MTR3 (Exosome component 6) (mRNA transport regulator 3 homolog) (hMtr3) (p11) (Q5RKV6)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus, nucleolus {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Exosome complex component RRP4
- Exosome complex component RRP40
- Exosome complex component RRP45
- Exosome complex component 10
- Exosome complex exonuclease RRP44
- Exosome complex component CSL4
- M-phase phosphoprotein 6
- Exosome complex component RRP43
- Exosome complex component RRP46
- DIS3-like exonuclease 1
Sequence:
MPGDHRRIRGPEESQPPQLYAADEEEAPGTRDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGPAGAGGEAPAALRGRLLCDFRRAPFAGRRRRAPPGGCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSLAPGPAPTWLLDPTRLEEERAAAGLTVALMPVLNQVAGLLGSGEGGLTESWAEAVRLGLEGCQRLYPVLQQSLVRAARRRGAAAQP
Protein: Centromere DNA-binding protein complex CBF3 subunit B (Centromere protein 3) (P40969)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters.
Subcellular location: Nucleus {ECO:0000305}. Chromosome, centromere.
Interaction partners:
- Suppressor of kinetochore protein 1
- Centromere DNA-binding protein complex CBF3 subunit C
- Centromere DNA-binding protein complex CBF3 subunit A
- Centromere-binding protein 1
- Histone H3-like centromeric protein CSE4
- Kinetochore-associated protein DSN1
- Chromosomal passenger complex protein BIR1
- Histone H3
- Very-long-chain enoyl-CoA reductase
- Histone H4
Sequence:
MFNRTTQLKSKHPCSVCTRRKVKCDRMIPCGNCRKRGQDSECMKSTKLITASSSKEYLPDLLLFWQNYEYWITNIGLYKTKQRDLTRTPANLDTDTEECMFWMNYLQKDQSFQLMNFAMENLGALYFGSIGDISELYLRVEQYWDRRADKNHSVDGKYWDALIWSVFTMCIYYMPVEKLAEIFSVYPLHEYLGSNKRLNWEDGMQLVMCQNFARCSLFQLKQCDFMAHPDIRLVQAYLILATTTFPYDEPLLANSLLTQCIHTFKNFHVDDFRPLLNDDPVESIAKVTLGRIFYRLCGCDYLQSGPRKPIALHTEVSSLLQHAAYLQDLPNVDVYREENSTEVLYWKIISLDRDLDQYLNKSSKPPLKTLDAIRRELDIFQYKVDSLEEDFRSNNSRFQKFIALFQISTVSWKLFKMYLIYYDTADSLLKVIHYSKVIISLIVNNFHAKSEFFNRHPMVMQTITRVVSFISFYQIFVESAAVKQLLVDLTELTANLPTIFGSKLDKLVYLTERLSKLKLLWDKVQLLDSGDSFYHPVFKILQNDIKIIELKNDEMFSLIKGLGSLVPLNKLRQESLLEEEDENNTEPSDFRTIVEEFQSEYNISDILS
Protein: Mitochondrial Ribosomal Protein, Large (O18180)
Organism: Caenorhabditis elegans
Interaction partners:
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS9m
- Ribosomal Protein, Small subunit
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS17
- Ribosomal protein
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein bS6m
Sequence:
MLSRTLRPISKVLRSSAKYSQAAGLPLNEGSPAPLPSEDRAISAKVSSLVEEIANLSLLDVSDLNWALKKRLNIPDQPLMAAAAAAPAAQAEAEAASDVPQKMTFTVKLTKFDDTKKIAIIKEIRNAIPGLNLVQAKKFVETAPVNVKEDLGKAEADELKAILEKAGATIEIV
Protein: Evasin P1156 (V5HBW0)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6 and CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MEVKTYAFLQIAVFIFLGMQIFASLTDAADDDNELFTVQYCGMNCTKDEGGTWTGCTGKKEGCKCYHESGKNYGLCLSTEYTDFSQYGNPSDSEIEAAKPKRSDTLSH
Protein: Beta-galactosidase 1 (Lactase 1) (EC 3.2.1.23) (Q9SCW1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- En/Spm-like transposon protein-like
- F13F21.11 protein
- Protein trichome birefringence-like 13
Sequence:
MGSKPNAMKNVVAMAAVSALFLLGFLVCSVSGSVSYDSRAITINGKRRILISGSIHYPRSTPEMWPDLIRKAKEGGLDVIQTYVFWNGHEPSPGKYYFEGNYDLVKFVKLVQQSGLYLHLRIGPYVCAEWNFGGFPVWLKYIPGISFRTDNGPFKAQMQRFTTKIVNMMKAERLFESQGGPIILSQIENEYGPMEYELGAPGRSYTNWAAKMAVGLGTGVPWVMCKQDDAPDPIINACNGFYCDYFSPNKAYKPKMWTEAWTGWFTKFGGPVPYRPAEDMAFSVARFIQKGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLERQPKWGHLKDLHRAIKLCEPALVSGEPTRMPLGNYQEAHVYKSKSGACSAFLANYNPKSYAKVSFGNNHYNLPPWSISILPDCKNTVYNTARVGAQTSRMKMVRVPVHGGLSWQAYNEDPSTYIDESFTMVGLVEQINTTRDTSDYLWYMTDVKVDANEGFLRNGDLPTLTVLSAGHAMHVFINGQLSGSAYGSLDSPKLTFRKGVNLRAGFNKIAILSIAVGLPNVGPHFETWNAGVLGPVSLNGLNGGRRDLSWQKWTYKVGLKGESLSLHSLSGSSSVEWAEGAFVAQKQPLTWYKTTFSAPAGDSPLAVDMGSMGKGQIWINGQSLGRHWPAYKAVGSCSECSYTGTFREDKCLRNCGEASQRWYHVPRSWLKPSGNLLVVFEEWGGDPNGITLVRREVDSVCADIYEWQSTLVNYQLHASGKVNKPLHPKAHLQCGPGQKITTVKFASFGTPEGTCGSYRQGSCHAHHSYDAFNKLCVGQNWCSVTVAPEMFGGDPCPNVMKKLAVEAVCA
Protein: MoaB/Mog domain-containing protein (G5EB65)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Molybdopterin synthase catalytic subunit
- Molybdenum cofactor sulfurase
- Aminotransferase class V domain-containing protein
- molybdopterin adenylyltransferase
- Radical SAM core domain-containing protein
- MOSC domain-containing protein
- Multifunctional tryptophan biosynthesis protein
- Adenylyltransferase and sulfurtransferase uba4
Sequence:
MAEQRLKAAILVVSDTAFQDPSSDRVFGTLIDVFPADGPWEKPITKIVPDDVLQIQRAVCDWTDSPSPVNLVLISGGTGFAVKDNTPEAVTPLLHRHAPGLVHGMIAASLKVTPFAMMARPVAGTRHKSLVITLPGSPKGAKENLEAVIKLLPHACTQAAGADSRTLHAGGIKKLEAEAGVKSESQHDHHHHHHHEHTHSHSHSHGHGHGHVVPRAHTTPSERRSNDPAAGATRRYRESPYPMLSVDEALRQVSAHTPEPEVIEVPVNIDLVGYVIAEDVYAAEAVPAYLASIVDGYAVIAPESPDDGHSTKGIFPVASITHANEEGALAPLEPGTIARITTGAPLPPNANAVVMVEDTLLASSTPDGKEEATVEILTGEIKPNENVRQPGSDVALGSRILQRGDLITPVGGEIGLLAATGTRTVKVFKKPVVGVLSTGDELVEHDDPRSLQGGQIRDSNRPSILSCLKSWGIPAVDLGIARDTPAGELEQSLRDALRGVGKSNTSVDVIITTGGVSMGELDLLKPTIERSLGGTIHFGRVSMKPGKPTTFATVPFKPTSSAAGQQERSSRLIFSLPGNPASALVTLNLFVLPSLHKLIGLGQKQAALGIAPALGLPLVAVTLSHAFPLDPKRTEYHRAIVTASPKDGRLYATSTGAEGVGQRSSRVGSLASANSLLVLQPGKGSIAQGSLVEALMMGPIVREGAAVAL
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13 (Q9P2W3)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 3
Sequence:
MEEWDVPQMKKEVESLKYQLAFQREMASKTIPELLKWIEDGIPKDPFLNPDLMKNNPWVEKGKCTIL
Protein: Thylakoid soluble phosphoprotein (Q8GT36)
Organism: Spinacia oleracea (Spinach)
Interaction partners:
Sequence:
MSSLPFVFGAAASSRVVTAAAAKGTAETKQEKSFVDWLLGKITKEDQFYETDPILRGGDVKSSGSTSGKKGGTTSGKKGTVSIPSKKKNGNGGVFGGLFAKKD
Protein: GPE1-BP (Q54AJ1)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSKLSQPATTPGVNGISVIHTQAHASGLQQVPQLVPAGPGGGGKAVPPSKQSKKSSPMDRNSDEYRQRRERNNMAVKKSRLKSKQKAQDTLQRVNQLKEENERLEAKIKLLTKELSVLKDLFLEHAHSLADNVQPISTETTATNSDNPGQ
Protein: Centrosomal protein of 104 kDa (Cep104) (Glycine-, glutamate- and thienylcyclohexylpiperidine-binding protein) (Gly-, L-Glu and TCP-binding protein) (GlyBP) (D3Z8X7)
Organism: Rattus norvegicus (Rat)
Function: Required for ciliogenesis and for structural integrity at the ciliary tip.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O60308}. Note=In interphase non-ciliated cells, localizes to the distal ends of both the mother and daughter centrioles. In ciliated cells, present at the distal end of the daughter centriole, but not on the mother centriole, and at the tip of primary cilium. Localization at the ciliary tip is also observed in motile cilia. Throughout S phase, associated with both mother and daughter centrioles in each centrosome. During metaphase and telophase, present at both spindle poles. {ECO:0000250|UniProtKB:O60308}.
Interaction partners:
- Centriolar coiled-coil protein 110
- Centrosomal protein 89
Sequence:
MPHKIGFVVVSSSGHEDGFSARELMIHAPTVSGWRSPKFCQFPQEIVLQMVERCRIRKLQLLAHQYMISSKVEFYISESLPEYLVPYQAERFRRLGYVSLCDNEKTGCKARELKSVYVDAVGQFLKLIFHQTTNKYNVNQVALVAINIIGDPADLGDESNTTCREKLIDHYLGHSPHNPEDPALDGTFAGRSDYISPLDDLAFDMYQDPEVAQIIRRLDERKREAAKKERYDHAKKLKQAIADLQKVGERLGRYEVEKRRAVEKEDYDLAKEKKQQMARYRAQVYEQLELHGLLQGEPEMQRPFALPLQPLASPSSPQHWKAVSSLPRTEELAAEDTCAGPILQEKPLASSPRHSAVDRSPPAAGPAPRSHVEALPYDERPLPVTRKQLEEPSAEPEVREADSDVRRRGVSAEPEPLTEKALREASSAIDTLGEALVAGAYSKMWSCREDALLALYKRLMEMPVGTQKEDLKNMLRASVFLIRRAIKDIVTSVFQASLKLLKMIITQYIPKHKLGKLDTTYCVERAIPLLLARTGDSSARLRVMALNFIQEMALFKEVRSLQLIPSYLVQPLKTNASVHLAMSQVDLLARLLRDLGTEGSGFTVDNVMKFAVSALEHRVYEVRETAVRIILDMYRQHPALTLEHLPPDDSTTRRNLLYKAIFEGFAKIDGRPTEAEGKTQKRVVTKEAEKQKKEETKALQGLSAAPRETQAGVQEKENEAVKLKNQDPQGRKAAPPDTPEIPDNHYLDNLCIFCGERNESFTEEGLDLHYWKHCLMLTRCDHCRQVVEISSLTEHLLTECDKRDGFGKCPRCSEAVPKEELPRHIKTKECNPAKSEKVANRCPLCHENFAPGEEAWKVHLMGSAGCTMNLRKTHILCKAPAPQQGKGPMASKSGTSAPKVGSKIPTPKGGLSKSSSRTHTRR
Protein: IQ domain-containing protein E (Q6PCQ0)
Organism: Mus musculus (Mouse)
Function: Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling. Required for proper limb morphogenesis (By similarity).
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:24582806}; Peripheral membrane protein {ECO:0000269|PubMed:24582806}; Cytoplasmic side {ECO:0000269|PubMed:24582806}. Note=The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner (PubMed:24582806). {ECO:0000269|PubMed:24582806}.
Interaction partners:
- EF-hand calcium-binding domain-containing protein 7
- Limbin
- Ubiquitin-like protein FUBI
- Tetratricopeptide repeat protein 23
- Transmembrane protein 143
Sequence:
MSLGTTDIASETGDDSLSAITFESDIESKTKRKSFHKPPSTSPKSPYYSKPRKVTSWRSLKTAGSMPLSSRMSLTPQKLWLGSSKQGSVAQPPSPTLTSEHAWTHPPSCTPDYLTEAVRAKRADLRRSGSHGHVSGTSVYREKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGWVITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPCSEERREAAIRTLQAQWKAHRRKKREAALDEAATVLQAAFRGHLARSKLVRSKVPDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQARFIASCCREIAASSQRETVSLTPSGSASPPSLRASPGVIRKELCASEELRETSASEPAPSVPYSAQGGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSPF
Protein: Protein c-Fos (Cellular oncogene fos) (Q6P0S4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Transcription factor Jun
- Transcription factor JunD
- JunB proto-oncogene, AP-1 transcription factor subunit a.
- JunB proto-oncogene, AP-1 transcription factor subunit b.
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase 8
- Stress-activated protein kinase JNK
- Stress-activated protein kinase JNK
- Nuclear factor of activated T-cells, cytoplasmic 2 isoform X1
- FBJ murine osteosarcoma viral oncogene homolog B
Sequence:
MMFTSLNADCDASSRCSTASPSGDSVGYYPLNQTQEFTDLSVSSASFVPTVTAISSCPDLQWMVQPMISSVAPSNGAAQSYNPSSYPKMRVTGAKTSNKRSRSEQLSPEEEEKKRVRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQNDIANLLKEKERLEFILAAHKPICKIPADASFPEPSSSPMGSISVPEIVTTSVVSSTPNTSITTSSSSLLFSSTASTDSFSSTTVKISDLEPTLEESLELLAKAELETARSVPDMDLSNSLYTQDWEPLYTPANTDLEPLCTPVVTCTPACTTYTSSFMFTYPENDVFPTSVHRRGSSSNDQSSDSLNSPTLLTL
Protein: Cyclin dependent kinase like 1 (A0A5H1ZRP5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKKFLESEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLHELDRYQRGVPEHLVKSITWQTLQAVNFCHKHNCIHRDVKPENILITKHSVIKLCDFGFARLLTGPSDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSTNQYFSGVKIPDPEDMEPLELKFPNISYPALGLLKGRVPIASRTE
Protein: [histone H3]-trimethyl-L-lysine(9) demethylase (EC 1.14.11.66) (F5GX28)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSEDHGAQNPSCKIMTFRPTMEEFKDFNKYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGSLRTILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDVFVRILQPERYELWKQGKDLTVLDHTRPTALTSPELSSWSASRASLKAKLLRRQISLKENRHWRKTEEERKPSLERKKEQTKRPGLSSHRKRSQPKKPKPEDPKFPGEGTAGAALLEEAGGSVKEEAGPEVDPEEEEEEPQPLPHGREAEGAEEDGRGKLRPTKAKSERKKKSFGLLPPQLPPPPAHFPSEEALWLPSPLEPPVLGPGPAAMEESPLPAPLNVVPPEVPSEELEAKPRPIIPMLYVVPRPGKAAFNQEHVSCQQAFEHFAQKGPTWKEPVSPMELTGPEDGAASSGAGRMETKARAGEGQAPSTFSKLKMEIKKSRRHPLGRPPTRSPLSVVKQEASSDEEASPFSGEEDVSDPDALRPLLSLQWKNRAASFQAERKFNAAAARTEPYCAICTLFYPYCQALQTEKEAPIASLGEGCPATLPSKSRQKTRPLIPEMCFTSGGENTEPLPANSYIGDDGTSPLIACGKCCLQVHASCYGIRPELVNEGWTCSRCAAHAWTAECCLCNLRGGALQMTTDRRWIHVICAIAVPEARFLNVIERHPVDISAIPEQRWKLKCVYCRKRMKKVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHKSGGHAVQLLRAVSLGQVVITKNRNGLYYRCRVIGAASQTCYEVNFDDGSYSDNLYPESITSRDCVQLGPPSEGELVELRWTDGNLYKAKFISSVTSHIYQVEFEDGSQLTVKRGDIFTLEEELPKRVRSRLSLSTGAPQEPAFSGEEAKAAKRPRVGTPLATEDSGRSQDYVAFVESLLQVQGRPGAPF
Protein: Pathogenesis-related thaumatin superfamily protein (Thaumatin-like protein; 9376-10898) (Q9C9U9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- CAP superfamily protein
- Polyadenylate-binding protein RBP45B
- Putative S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase; 41514-39166
- Gb|AAF63169.1/surp domain-containing protein)
Sequence:
MTNEKCEVALPLKLKSEKPSMASSSSLFLLPLLLLVSQASASTVIFYNKCTYTVWPGIQPSSGQSLLAGGGFKLSPNRAYTLQLPPLWSGRFWGRHGCSFDRSGRGRCATGDCGGSFLCNGAGGVPPATLAEITLGHDMDFYDVSLVDGYNLAMSIMPVKGTGKCTYAGCVSDLNRMCPVGLQVRSRDGTQVVACKSACSAFNSPRYCCTGLFGNPQSCKPTAYSKIFKVACPKAYSYAYDDPTSIATCSKANYVVTFCPHRGR
Protein: Non-specific ribonucleoside hydrolase RihC (EC 3.2.-.-) (Purine/pyrimidine ribonucleoside hydrolase) (P22564)
Organism: Escherichia coli (strain K12)
Function: Hydrolyzes both purine and pyrimidine ribonucleosides with a broad-substrate specificity with decreasing activity in the order uridine, xanthosine, inosine, adenosine, cytidine, guanosine.
Interaction partners:
- Carbamoyl phosphate synthase small chain
- 4-hydroxy-tetrahydrodipicolinate reductase
- Ribokinase
- FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase
- Uncharacterized protein YjgR
Sequence:
MRLPIFLDTDPGIDDAVAIAAAIFAPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNAEIPLAQGAAVPLVRAPRDAASVHGESGMAGYDFVEHNRKPLGIPAFLAIRDALMRAPEPVTLVAIGPLTNIALLLSQCPECKPYIRRLVIMGGSAGRGNCTPNAEFNIAADPEAAACVFRSGIEIVMCGLDVTNQAILTPDYLSTLPQLNRTGKMLHALFSHYRSGSMQSGLRMHDLCAIAWLVRPDLFTLKPCFVAVETQGEFTSGTTVVDIDGCLGKPANVQVALDLDVKGFQQWVAEVLALAS
Protein: Reticulon-3 (Q9ES97)
Organism: Mus musculus (Mouse)
Function: May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules. Acts also as an inflammation-resolving regulator by interacting with both TRIM25 and RIGI, subsequently impairing RIGI 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B inhibition (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15350194}; Multi-pass membrane protein {ECO:0000269|PubMed:15350194}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O95197}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Beta-secretase 1
- Reticulon-4
- Beta-secretase 2
- Translocation protein SEC62
- Atlastin-3
- Cell cycle progression protein 1
- Atlastin-1
- Reticulophagy regulator 1
- Microtubule-associated protein 1 light chain 3 beta
- Testis-expressed protein 264 homolog
Sequence:
MAESSAATQSPSVSSSSSGAEPSALGGGGGSPGACPALGAKSCGSSCADSFVSSSSSQPVSIFSTSQAGLSSLCSDEPPSKSMTSSFLSSSEIHNPDPTTPLGEKSETLGSQFVLAKGKDPLVLLDKKKLDSPQGTNKDRVDAPVSLATGIPCSHPSIPDSFPEQPAFLSKEIGPAEEWVVKDQEPKNPNKVPDGEDRSALDFGQSKAEHICTYSLSPSELPVASVEKDSPESPFEVIIDKATFDREFKDLYKENPNDLGGWAAHGDRESPADLLEMNDKLFPLRNKEAGRYPSSVLLGRQFSHTTAALEEVSRCVNDMHNFTNEILTWDLDPQAKQQANKTSCTTESTGLDRSELRSEIPVINLKTNPQQKMPVCSFNGSTPITKSTGDWTEAFTEGKPVRDYLSSTKEAGGNGVPGSSQLHSELPGSMPEKWVSGSGAATVEVTLPNLRGAWPNSVMGEVTEVDSSGESDDTVIEDITEKPDSLPSAAAKTSEREIKETPSRETVRSEMCENSEQPQAQPETPTQKSLEGEVASQVPNTLNEVTPEKLDMTNNPKVCSAAPPSVLNETGFSLTVPASAKLESLLGKYVEDTDGSSPEDLMAVLTGAEEKGIVDKEEGDVLEAVLEKIADFKNTLPVELLHESELSGSETKNIKSKYSEDSRETTGGAPTMSPDLEQEQLTIRAIKELGERQAEKVQDEGISSGGKLKQTFAPQSGPQSSSDILEHTDVKTGSDLGIPKNPTIIKNTRIDSISSLTKTEMVNKNVLARLLSDFPVHDLIFWRDVKKTGFVFGTTLIMLLSLAAFSVISVVSYLILALLSVTISFRVYKSVIQAVQKSEEGHPFKAYLDVDITLSSEAFHNYMNAAMVHVNKALKLIIRLFLVEDLVDSLKLAVFMWLMTYVGAVFNGITLLILAELLVFSVPIVYEKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE