wanglab/gogpt-training-data huggingface dataset:
Protein: Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form] (P16599)
Organism: Rattus norvegicus (Rat)
Function: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000250}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor receptor superfamily member 1B
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- TNF receptor-associated factor
- Transcription factor Jun
- Transcription factor p65
- TNF receptor-associated factor 6
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- FAS-associated death domain protein
- Nuclear factor NF-kappa-B p105 subunit
Sequence:
MSTESMIRDVELAEEALPKKMGGLQNSRRCLCLSLFSFLLVAGATTLFCLLNFGVIGPNKEEKFPNGLPLISSMAQTLTLRSSSQNSSDKPVAHVVANHQAEEQLEWLSQRANALLANGMDLKDNQLVVPADGLYLIYSQVLFKGQGCPDYVLLTHTVSRFAISYQEKVSLLSAIKSPCPKDTPEGAELKPWYEPMYLGGVFQLEKGDLLSAEVNLPKYLDITESGQVYFGVIAL
Protein: Gastrin-releasing peptide (GRP) [Cleaved into: Neuromedin-C (GRP-(18-27)) (GRP-10) (GRP18-27)] (Q863C3)
Organism: Bos taurus (Bovine)
Function: Stimulates the release of gastrin and other gastrointestinal hormones (By similarity). Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior (By similarity). Contributes primarily to nonhistaminergic itch sensation (By similarity). In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear (By similarity). In another study, shown to act on vasoactive intestinal peptide (VIP)-expressing cells in the auditory cortex, most likely via extrasynaptic diffusion from local and long-range sources, to mediate disinhibition of glutamatergic cells via VIP cell-specific GRPR signaling which leads to enhanced auditory fear memories (By similarity). Contributes to the regulation of food intake (By similarity). Inhibits voltage-gated sodium channels but enhances voltage-gated potassium channels in hippocampal neurons (By similarity). Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:2755876}. Secreted {ECO:0000305|PubMed:2755876}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q8R1I2}. Note=In neurons of the retrotrapezoid nucleus/parafacial respiratory group, expressed on neuron projections which project into the pre-Botzinger complex. {ECO:0000250|UniProtKB:Q8R1I2}.
Interaction partners:
- Gastrin-releasing peptide receptor
- Neuromedin-B receptor
- Bombesin receptor subtype-3
- Pro-glucagon
- Signal peptidase complex subunit 2
- Neurotensin/neuromedin N
- Gastrin
- Signal peptidase complex subunit 3
- Somatostatin
- Cholecystokinin
Sequence:
MRGREVPLVLLALVLCLAPRGWAAPVTAGRGGALAKMYTRGNHWAVGHLMGKKSVAESPQLHEEESLKEQLREYAQWEEATRNLLSLLQAKGARGHQMPPWEPLSIHQPAWDSEDVSNFKDTGPQHEGRNPQLN
Protein: Putative FAD-containing monooxygenase MymA (EC 1.14.13.-) (P9WNF7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH.
Interaction partners:
- Putative oxidoreductase SadH
- Putative acetyl-hydrolase LipR
- Probable diacyglycerol O-acyltransferase Tgs4
- Long-chain-fatty-acid--CoA ligase FadD13
- Putative diacyglycerol O-acyltransferase Rv3087
- Putative alcohol dehydrogenase D
- HTH-type transcriptional regulator VirS
- FAD-containing monooxygenase EthA
- R2-like ligand binding oxidase
Sequence:
MNQHFDVLIIGAGLSGIGTACHVTAEFPDKTIALLERRERLGGTWDLFRYPGVRSDSDMFTFGYKFRPWRDVKVLADGASIRQYIADTATEFGVDEKIHYGLKVNTAEWSSRQCRWTVAGVHEATGETRTYTCDYLISCTGYYNYDAGYLPDFPGVHRFGGRCVHPQHWPEDLDYSGKKVVVIGSGATAVTLVPAMAGSNPGSAAHVTMLQRSPSYIFSLPAVDKISEVLGRFLPDRWVYEFGRRRNIAIQRKLYQACRRWPKLMRRLLLWEVRRRLGRSVDMSNFTPNYLPWDERLCAVPNGDLFKTLASGAASVVTDQIETFTEKGILCKSGREIEADIIVTATGLNIQMLGGMRLIVDGAEYQLPEKMTYKGVLLENAPNLAWIIGYTNASWTLKSDIAGAYLCRLLRHMADNGYTVATPRDAQDCALDVGMFDQLNSGYVKRGQDIMPRQGSKHPWRVLMHYEKDAKILLEDPIDDGVLHFAAAAQDHAAA
Protein: Ankyrin 2 (A0A5F9ZHL3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGRASPCLERDNSSFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEVTLCEPSILSSTSQFQAEPVEGRRVSKVVKTTVVLGERMEKHLGDSSLATDLPSAKDDFEEDNNE
Protein: Tubulin polyglutamylase TTLL5 (EC 6.3.2.-) (SRC1 and TIF2-associated modulatory protein) (STAMP protein) (Tubulin--tyrosine ligase-like protein 5) (Q6EMB2)
Organism: Homo sapiens (Human)
Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Preferentially mediates ATP-dependent initiation step of the polyglutamylation reaction over the elongation step. Preferentially modifies the alpha-tubulin tail over a beta-tail (By similarity). Required for CCSAP localization to both polyglutamylated spindle and cilia microtubules. Increases the effects of transcriptional coactivator NCOA2/TIF2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:24791901}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8CHB8}. Nucleus {ECO:0000269|PubMed:17116691}. Cytoplasm {ECO:0000269|PubMed:17116691}. Note=Localized to the base of the connecting cilium between the basal body and the adjacent daughter centriole of the cilium. In osteosarcoma cells, found in both cytoplasm and nucleus in the absence of steroid but located exclusively in the nucleus in the presence of steroid. {ECO:0000250|UniProtKB:Q8CHB8, ECO:0000269|PubMed:24791901}.
Interaction partners:
- Coiled-coil domain-containing protein 14
- TSC22 domain family protein 3
Sequence:
MPIVMARDLEETASSSEDEEVISQEDHPCIMWTGGCRRIPVLVFHADAILTKDNNIRVIGERYHLSYKIVRTDSRLVRSILTAHGFHEVHPSSTDYNLMWTGSHLKPFLLRTLSEAQKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKAFHILPQTFLLPAEYAEFCNSYSKDRGPWIVKPVASSRGRGVYLINNPNQISLEENILVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGAKNIRNQFMHLTNYSVNKKSGDYVSCDDPEVEDYGNKWSMSAMLRYLKQEGRDTTALMAHVEDLIIKTIISAELAIATACKTFVPHRSSCFELYGFDVLIDSTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVVGFVCQDPAQRASTRPIYPTFESSRRNPFQKPQRCRPLSASDAEMKNLVGSAREKGPGKLGGSVLGLSMEEIKVLRRVKEENDRRGGFIRIFPTSETWEIYGSYLEHKTSMNYMLATRLFQDRMTADGAPELKIESLNSKAKLHAALYERKLLSLEVRKRRRRSSRLRAMRPKYPVITQPAEMNVKTETESEEEEEVALDNEDEEQEASQEESAGFLRENQAKYTPSLTALVENTPKENSMKVREWNNKGGHCCKLETQELEPKFNLMQILQDNGNLSKMQARIAFSAYLQHVQIRLMKDSGGQTFSASWAAKEDEQMELVVRFLKRASNNLQHSLRMVLPSRRLALLERRRILAHQLGDFIIVYNKETEQMAEKKSKKKVEEEEEDGVNMENFQEFIRQASEAELEEVLTFYTQKNKSASVFLGTHSKISKNNNNYSDSGAKGDHPETIMEEVKIKPPKQQQTTEIHSDKLSRFTTSAEKEAKLVYSNSSSGPTATLQKIPNTHLSSVTTSDLSPGPCHHSSLSQIPSAIPSMPHQPTILLNTVSASASPCLHPGAQNIPSPTGLPRCRSGSHTIGPFSSFQSAAHIYSQKLSRPSSAKAGSCYLNKHHSGIAKTQKEGEDASLYSKRYNQSMVTAELQRLAEKQAARQYSPSSHINLLTQQVTNLNLATGIINRSSASAPPTLRPIISPSGPTWSTQSDPQAPENHSSSPGSRSLQTGGFAWEGEVENNVYSQATGVVPQHKYHPTAGSYQLQFALQQLEQQKLQSRQLLDQSRARHQAIFGSQTLPNSNLWTMNNGAGCRISSATASGQKPTTLPQKVVPPPSSCASLVPKPPPNHEQVLRRATSQKASKGSSAEGQLNGLQSSLNPAAFVPITSSTDPAHTKI
Protein: Thiocillin GE37468 (Antibiotic GE37468) (P0C8P9)
Organism: Streptomyces sp
Function: Has bacteriocidal activity against both aerobic and anaerobic Gram-positive bacteria. Inhibits growth of B.subtilis (MIC=0.047 ug/ml) and methicillin-resistant S.aureus (MRSA) (MIC=0.047 ug/ml). Has poor activity against Gram-negative bacteria, with the exception of B.fragilis. Inhibits bacterial protein biosynthesis by acting on elongation factor Tu (EF-Tu). Full antibiotic activity depends on the presence of the modified residue Ile-50.
Subcellular location: Secreted {ECO:0000269|PubMed:7592021}.
Interaction partners:
Sequence:
MGNNEEYFIDVNDLSIDVFDVVEQGGAVTALTADHGMPEVGASTNCFCYICCSCSSN
Protein: Protein S100 (S100 calcium-binding protein) (Q9PSF6)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
Sequence:
MSDLQKGMALLISTFHKYSGEEGDKCTLTKGELKDLLTKELGGAFGNCSDQATLDKIFKDLDTNADGVVDFQEYATMVACTTMLCNKSLSKK
Protein: Multiple organellar RNA editing factor 8, chloroplastic/mitochondrial (RNA editing-interacting protein 1) (Q9LKA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in organellar RNA editing. Required for the processing of numerous RNA editing sites in mitochondria and plastids. Binds to the plastid RARE1 factor, a pentatricopeptide repeat-containing protein involved in RNA editing.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:22566615, ECO:0000269|PubMed:25583991, ECO:0000269|PubMed:26578708}. Plastid, chloroplast {ECO:0000269|PubMed:22566615, ECO:0000269|PubMed:25583991, ECO:0000269|PubMed:28213559}. Note=Dual targeting to mitochondria and chloroplasts. {ECO:0000269|PubMed:22566615, ECO:0000269|PubMed:25583991}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At5g13270
- Pentatricopeptide repeat-containing protein At3g02330, mitochondrial
- Putative pentatricopeptide repeat-containing protein At3g11460, mitochondrial
- Pentatricopeptide repeat-containing protein At4g14050, mitochondrial
- Protoporphyrinogen oxidase 1, chloroplastic
- Glycine-rich RNA-binding protein 3, mitochondrial
- Organelle RRM domain-containing protein 6
- Pentatricopeptide repeat-containing protein DWY1, chloroplastic
- NAD
- Zinc finger protein VAR3, chloroplastic
Sequence:
MATHTISRSILCRPAKSLSFLFTRSFASSAPLAKSPASSLLSRSRPLVAAFSSVFRGGLVSVKGLSTQATSSSLNDPNPNWSNRPPKETILLDGCDFEHWLVVVEPPQGEPTRDEIIDSYIKTLAQIVGSEDEARMKIYSVSTRCYYAFGALVSEDLSHKLKELSNVRWVLPDSYLDVRNKDYGGEPFIDGKAVPYDPKYHEEWIRNNARANERNRRNDRPRNNDRSRNFERRRENMAGGPPPQRPPMGGPPPPPHIGGSAPPPPHMGGSAPPPPHMGQNYGPPPPNNMGGPRHPPPYGAPPQNNMGGPRPPQNYGGTPPPNYGGAPPANNMGGAPPPNYGGGPPPQYGAVPPPQYGGAPPQNNNYQQQGSGMQQPQYQNNYPPNRDGSGNPYQG
Protein: Leucine-rich repeat protein (LRRP) (Q57XU4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGIGQSRELLGKVGEEHVFVCTNYEELLATLRKLQSCSELRSSQGAVKFEGSLPTVANSGTPTQWEETKCRPVSKGSCTLLGSGVYRGSLRFLPPSFLTDTTAKPLEEVHIPNHYMGDAGLISGHEAVLQTLANSPGLRSLNISYNALTHVSIEALLGKAPHNGAHDDNGFPGGFLPPNLLSLNFAGNRAGRVGCERLAEFLETDPPLRALSLYNNELYDDDVEPLLRGLRVNTRLRQLNLDCNYLTGGFLQQLIDVLRVNRQLAVVMFDGPYDMNTFARLKELKPVEAVPDKAEDPAGHARALLRNEMLCHDLAGRPPFPTDLVQEVEAILKPRCARYVDELREERERAYQEAKNTDEMLEVARRYRDASCDTCGGEATDLSHQEECDSADKSKSDNGTQGPQEEEDRDEDGEREQGTEGEEKQEEIETGAGNRDGGFGFFRPPLRGKDASRNGSVAPVAAPLSCLRPMPPYAERKRQSATFFPGLLLSPVEGGSSASHSMLSNTEARRDKSPASGEHRMEETGRTTANSKSSVLPRKELTNGFDRLVLAPLSEAPRSKTIWKTVTGPPCRLRACWCDARADIVPYANVLHYHCKHEQLTNEAGYEMEPCRLTTGKSSVSRGRPGRLPLKEKKGSGPEWSHTSRATIRPHSGRDCATPSAGGYAGSGPSGRTVYEGCKATSHRCESIGFYGRPKPDRRSVVFFSGQHPMLARGLKE
Protein: Mitogen-activated protein kinase kinase kinase 7 interacting protein 1, isoform CRA_f (cDNA FLJ78598, highly similar to Homo sapiens mitogen-activated protein kinase kinase kinase 7 interacting protein 1 (MAP3K7IP1), transcript variant alpha, mRNA) (cDNA, FLJ92811, Homo sapiens mitogen-activated protein kinase kinase kinase 7interacting protein 1 (MAP3K7IP1), mRNA) (A8K6K3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAQRRSLLQSEQQPSWTDDLPLCHLSGVGSASNRSYSADGKGTESHPPEDSWLKFRSENNCFLYGVFNGYDGNRVTNFVAQRLSAELLLGQLNAEHAEADVRRVLLQAFDVVERSFLESIDDALAEKASLQSQLPEGVPQHQLPPQYQKILERLKTLEREISGGAMAVVAVLLNNKLYVANVGTNRALLCKSTVDGLQVTQLNVDHTTENEDELFRLSQLGLDAGKIKQVGIICGQESTRRIGDYKVKYGYTDIDLLSAAKSKPIIAEPEIHGAQPLDGVTGFLVLMSEGLYKALEAAHGPGQANQEIAAMIDTEFAKQTSLDAVAQAVVDRVKRIHSDTFASGGERARFCPRHEDMTLLVRNFGYPLGEMSQPTPSPAPAAGGRVYPVSVPYSSAQSTSKTSVTLSLVMPSQGQMVNGAHSASTLDEATPTLTNQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDGRVEPYVDFAEFYRLWSVDHGEQSVVTAP
Protein: RE41741p (Q8MS21)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MCCSCCGVTQQKAWVFGLGTFFAVSGLLAIICWPGFIDSGIMKALPLTPTSKTFEKWEELPIPVYVYMYLWNWTNAADVQANGVKPIFAQLGPYVYREERKKMDLEWHDNGTVTFNPRRTWFWEEELSGGKQTDLITAPHLPSLAASNQMRNSNVFLKFMFNEALNANGGHLFVTHTAAEWLFESFYDEFLHYAMTLNNPLVPKIESDHFAWFLNRNGSKDFEGPFTVHTGVGDIKEMGEIKYWKGQNHTGWYDGECGRLNGSTTDLFVPDEPKGEGFDHLHSGYLSDHKS
Protein: Tropomyosin TpmA (Eurofung) (Q5B194)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- D-lactate dehydratase
- Rho GTPase activator Rga
- Actin, gamma
- Myosin II homolog
- Calmodulin, putative
- Uncharacterized protein
- BZIP domain-containing protein
- Actin-related protein
- Alpha-actinin, sarcomeric
- Kinesin-like protein
Sequence:
MDRIKEKMNALRLEADEAHEKNEELKARVKTLEQENLAKEQEITSLTHRNQLLEAEVEKLESSAKEAKDAASQSAQHDTQNEALQRRIQLLEEEAEEADRNLRETNEKLRQTDVKAGHYERKVQALETSRDEWERKYEEMAAKHESLKKELAELELSLNSV
Protein: NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier) (Q9Y6K9)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much higher affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14651848, ECO:0000269|PubMed:24586164}. Nucleus {ECO:0000269|PubMed:14651848}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000269|PubMed:14651848}.
Interaction partners:
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- TNF receptor-associated factor 6
- Ubiquitin carboxyl-terminal hydrolase CYLD
- B-cell lymphoma/leukemia 10
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Tumor necrosis factor
- Interleukin-1 receptor-associated kinase 4
- Receptor-interacting serine/threonine-protein kinase 1
- Interleukin-1 receptor-associated kinase 1
- TNF receptor-associated factor 2
Sequence:
MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
Protein: UDP-glycosyltransferase 74G1 (EC 2.4.1.-) (Q6VAA6)
Organism: Stevia rebaudiana (Stevia) (Eupatorium rebaudianum)
Function: Involved in the biosynthesis of steviol glycosides in leaves. Converts steviol to the mono-glycoside steviolmonoside. Converts the mono-glycoside steviolmonoside to the bi-glycoside rubusoside. Converts the bi-glycoside steviolbioside to the tri-glycoside stevioside. Converts the tri-glycoside rebaudioside B to the tetra-glycoside rebaudioside A.
Interaction partners:
Sequence:
MAEQQKIKKSPHVLLIPFPLQGHINPFIQFGKRLISKGVKTTLVTTIHTLNSTLNHSNTTTTSIEIQAISDGCDEGGFMSAGESYLETFKQVGSKSLADLIKKLQSEGTTIDAIIYDSMTEWVLDVAIEFGIDGGSFFTQACVVNSLYYHVHKGLISLPLGETVSVPGFPVLQRWETPLILQNHEQIQSPWSQMLFGQFANIDQARWVFTNSFYKLEEEVIEWTRKIWNLKVIGPTLPSMYLDKRLDDDKDNGFNLYKANHHECMNWLDDKPKESVVYVAFGSLVKHGPEQVEEITRALIDSDVNFLWVIKHKEEGKLPENLSEVIKTGKGLIVAWCKQLDVLAHESVGCFVTHCGFNSTLEAISLGVPVVAMPQFSDQTTNAKLLDEILGVGVRVKADENGIVRRGNLASCIKMIMEEERGVIIRKNAVKWKDLAKVAVHEGGSSDNDIVEFVSELIKA
Protein: Cysteine-rich secretory protein 1 (CRISP-1) (AEG-like protein) (ARP) (Acidic epididymal glycoprotein homolog) (P54107)
Organism: Homo sapiens (Human)
Function: May have a role in sperm-egg fusion and maturation.
Subcellular location: Note=Located in the lumen and epithelium of distal ductus efferentes and epididymal ducts, and on the postacrosomal region of the sperm head.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MEIKHLLFLVAAACLLPMLSMKKKSARDQFNKLVTDLPNVQEEIVNIHNALRRRVVPPASNMLKMSWSEEAAQNARIFSKYCDMTESNPLERRLPNTFCGENMHMTSYPVSWSSVIGVWYSESTSFKHGEWTTTDDDITTDHYTQIVWATSYLIGCAIASCRQQGSPRYLYVCHYCHEGNDPETKNEPYKTGVPCEACPSNCEDKLCTNPCIYYDEYFDCDIQVHYLGCNHSTTILFCKATCLCDTEIK
Protein: Truncated formate dehydrogenase 2 (NAD-dependent formate dehydrogenase 2) (P0CF35)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MVVINKQLMVSGILPAWLKNEYDLEDKIISTVGAGRIGYRVLERLVAFNPKKLLYYDYQELPAEAINRLNEASKLFNGRGDIVQRVEKLEDMVAQSDVVTINCPLHKDSRGLFNKKLISHMKDGAYLVNTARGAICVAEDVAEAVKSGKLAGYGGDVWDKQPAPKDHPWRTMDNKDHVGNAMTVHISGTSLHAQKRYAQGVKNILNSYFSKKFDYRPQDIIVQNGSYATRAYGQKK
Protein: Chaperonin (Q877G8)
Organism: Methanococcus maripaludis (Methanococcus deltae)
Interaction partners:
Sequence:
MSQQPGVLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAEKLRGAPDMGDMGGMPGMGGMPGMM
Protein: Interferon induced transmembrane protein 2 (E9PQN9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLKEEQEVAMLGVPHNPAPPMSTVIHIRSETSVPDHVVWSLFNTLFMNTCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGIFMTILLIIIPVLVVQAQR
Protein: DNA polymerase epsilon subunit B (DNA polymerase II subunit 2) (O94263)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA polymerase epsilon catalytic subunit A
- Cell division control protein 45 homolog
- DNA polymerase epsilon subunit D
- DNA replication complex GINS protein psf1
- DNA replication licensing factor mcm5
- DNA replication complex GINS protein sld5
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm2
- DNA replication complex GINS protein psf2
Sequence:
MNNSITDSVEKKPEQVSFEVQPNALRPVAFHVFTRKYDLNINRDSLQELASFVSKKCGSQWRSQCEPLLDEIAKTWKRVHETQPIVTRPLLIPVLANLNVPHEVRVSSLARVQTLETTGSFLNSSNSEIRETIKNEKYFRVLDAFKMPKFKYDSSRKVFVLSKQSPTLMASASACTDMLNRRFNVVYSRILRNESFQTPSFSGSFSQTGTYQLTPIRNLLGRAGNTFLLFGLLTIAPDGTLWLEDLDSQVQLDVSQAEQGFGLFCPGCLVLVNGQFLSSGLFLVFELGHPPIERRDASLKALNNLDILGLNMDAKQLALLRHAEQAYQSQAFVCISEVHLDNHQTFYALEKIFQKYESSEAVPFCIILCGSFMSSAFHNSGSSIQYKEGFNKLAASLEKFPKICEKTKFIFVPGPNDPWTTNGISLMPKHSIPLHFVNRIQRVCKHTIFASNPCRIIFFSQEVLIYRDDISGRFQRNSLKFGKTPQGTSNINSIPLAEQQVHQQRKLVKTVLDQSHLSPFPSRTRPILWDFDYALSVFPLPSCMGLIDSESSAFDVHYGGCPTFNPGALLLGVHYNWQEVFPVKKEIITHKERI
Protein: WD-40 repeat-containing protein MSI3 (O22469)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- DNA damage-binding protein 1a
- Lysine-specific demethylase ELF6
- Histone H4
- DDT domain-containing protein PTM
- PHD finger family protein
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- PHD-finger and DNA binding domain-containing protein
- DNA damage-binding protein 1b
- Transducin/WD40 repeat-like superfamily protein
Sequence:
MAAEEGKDEAGLDQVEEEFSIWKRNTPFLYDLMISHPLEWPSLTLHWVPSTPIPYSKDPYFAVHKLILGTHTSGGAQDFLMVADVVIPTPDAEPGLGGRDQEPIVPKVEIKQKIRVDGEVNRARCMPQKPTLVGAKTSGSEVFLFDYARLSGKPQTSECDPDLRLMGHEQEGYGLAWSSFKEGYLLSGSQDQRICLWDVSATATDKVLNPMHVYEGHQSIIEDVAWHMKNENIFGSAGDDCQLVIWDLRTNQMQHQVKVHEREINYLSFNPFNEWVLATASSDSTVALFDLRKLTAPLHVLSKHEGEVFQVEWDPNHETVLASSGEDRRLMVWDINRVGDEQLEIELDAEDGPPELLFSHGGHKAKISDFAWNKDEPWVISSVAEDNSLQVWQMAESIYREDDEDEDDDDEGNQNAQHSNENQK