wanglab/gogpt-training-data huggingface dataset:
Protein: U3 small nucleolar RNA-associated protein 13 C-terminal domain-containing protein (Q387K5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- CCAAT-binding factor domain-containing protein
- Uncharacterized protein
- Periodic tryptophan protein 2, putative
- U3 small nucleolar ribonucleoprotein protein MPP10, putative
- Nucleolar RNA binding protein, putative
- KRR1 small subunit processome component
- U3 small nuclear ribonucleoprotein
- Bms1-type G domain-containing protein
- U3 small nucleolar RNA-associated protein 6 N-terminal domain-containing protein
- HEAT repeat-containing protein 1
Sequence:
MEGKNCFRTQWSQVPLYSGGNIASLLLLPNSQISSSLHSPCLNGVECLVAACGDTINVLRASDGERLASYTLPVEDVILRIDAVTVAPIAKPSATTKHSHGSVADGKSRKTKRDEVRDGEDTKVVDAAVPCGSYIAVGTRSLQIYVLRVEGAYPNLVEVGETKEGGDGGDQRIISSSVTKAVSDTNLICTLSPLRSWTASQQAISVVQFTFDGSHLVSGSTDGGVKVWDVFQHYLTHNLHSPSACLAHSFYVNSAKEFICVGSFEGHVAVFDFVEKTLVAHARPHVAAVEAICLTADNKHLLSVGRDRKVVINKMTKTGLEELRAVVVKEHVSSALFESAFRLHIGAMDGVISTYNVSVTEPLQLSRRRRKVGSDVEESDGELAVRSLVVANKPRGTHEVGLLHGVVEDDNPSRLYTADASFNISLLVPHPEKATYVPDVTLVGFLDQVLDVKLFPPHSPIHRVVVTNSKDLRCYPSQGCLSSVCLSGHSDIVLTCAVSVDTCLIATAGKDCTVRFWSTETWSTIAIGEKGHNADITFISFNAKQSDSYFLLFSVGTDENLCLWDVGTHVLPLVTKRKSSSEETLPITFTHRAGINSAHEGSIHTLAVAPNDQYVATAGKDKNVNLWTVSGKKLFRDASLKGHRRAVSSLAFSPTDRVLASASNDGSVRLWSLVSLTCVKALQVDRIPVLQLSFFNGGTQLVTGNAEGVLRVWAISVAEVVWSGETHEEKIWALCVSEPEGGNITFISGSADGVLIATEDYTAEEAERVRHERRDVILKEQELANALRKGEYVEAFMLALKLNHPRNLRQVVLRWSIKDAKGCEESLCKVVLPALNEEQLVRLLQFTREWITNARHCGVASLVIHTVLRAFHFSTLAEMPAISKVLEALLAYTQRHTHRVHDMLRRTYYIDYVTRSLVPPELTSQPPFVHSLASAARPPAKMQRREKT
Protein: Glutamate decarboxylase 2 (EC 4.1.1.15) (65 kDa glutamic acid decarboxylase) (GAD-65) (Glutamate decarboxylase 65 kDa isoform) (Q05683)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the production of GABA.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8999827}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q05329}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q05329}; Lipid-anchor {ECO:0000250|UniProtKB:Q05329}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q05329}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05329}; Cytoplasmic side {ECO:0000250|UniProtKB:Q05329}. Note=Associated to cytoplasmic vesicles. In neurons, cytosolic leaflet of Golgi membranes and presynaptic clusters. {ECO:0000250|UniProtKB:Q05329}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- 4-aminobutyrate aminotransferase, mitochondrial
- Glutamate decarboxylase 1
- Glutamate dehydrogenase 1, mitochondrial
- Glutamine synthetase
- Glutaminase liver isoform, mitochondrial
- Glutaminase kidney isoform, mitochondrial
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Alpha-aminoadipic semialdehyde dehydrogenase
Sequence:
MASPGSGFWSFGSEDGSGDPENPGTARAWCQVAQKFTGGIGNKLCALLYGDSEKPAESGGSVTSRAATRKVACTCDQKPCSCPKGDVNYALLHATDLLPACEGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILTHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMLIARYKMFPEVKEKGMAAVPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEVKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHIDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWFVPPSLRVLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
Protein: GATOR2 complex protein Mio (Protein missing oocyte) (Q9VQ89)
Organism: Drosophila melanogaster (Fruit fly)
Function: An essential component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway. The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation. GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation and growth under nutrient replete conditions and during female oocyte development. This component is required for activating TORC1 specifically in germline cells to promote cell growth and maintain the oocyte fate. GATOR1 and GATOR2 act at different stages of oogenesis to regulate TORC1 in order to control meiotic entry and promote oocyte growth and development. After exactly four mitotic cyst divisions, the GATOR1 complex members (Iml1, Nprl2 and Nprl3) down-regulate TORC1 to slow cellular metabolism and promote the mitotic/meiotic transition. At later stages of oogenesis, the mio and Nup44A components of the GATOR2 complex inhibit GATOR1 and thus activate TORC1 to promote meiotic progression, and drive oocyte growth and development. In addition to its role in the regulation of the TORC1 complex, functions independently of TORC1 to prevent the inappropriate accumulation of autolysosomes in germline tissues.
Subcellular location: Nucleus {ECO:0000269|PubMed:14973288}. Lysosome {ECO:0000269|PubMed:25512509}. Note=Accumulates in pro-oocyte nuclei in early prophase of meiosis I (PubMed:14973288). In egg chambers, detected in lysosomes and autolysosomes of both fed and starved females (PubMed:25512509). {ECO:0000269|PubMed:14973288, ECO:0000269|PubMed:25512509}.
Interaction partners:
- Protein SEC13 homolog
- Nucleoporin seh1
- GATOR complex protein Iml1
- GATOR complex protein NPRL2
- GATOR2 complex protein Wdr24
- GATOR2 complex protein Wdr59
- GATOR complex protein NPRL3
- GH04846p
- FI04419p
- GH16429p
Sequence:
MSGNTHGLSWFPHFPDKFVSWGQEIHLYEVRRKDDHSQKSRLPYISVNYLANESRYQYARCVAASYHSDQPIIAVGLADGKVGICNFRDTYDSSWEYTPRQQRMCTCLAWNELDANILAIGHDRHRNDTCITIWDIERGVPKETANFFGVGESANSICWDRNHRTVIAGMSQKMIKLFDLRQSNATCQSIQTKTVQGLSVSPNGNYLCSYVDSVITLWDPRNIKSPLRQIQSSKNHLQIAWCPTRTSLLSSLQRDSSYITLYDIRSVDTDNSGEIYHVKRQISPFPARYQHSGKFSFVNCLSWHSRDFERALLLADALNILDFRLPATLHTAHSNRRKLPLLMQRPLYTPASPTSTAATPTQQQPTSSCSTNSGSSLDFSTPGGSPFNVDLLKPELFELDLVDETRQRALEDYGIKPDNKRFGELHLTPYLRNVWSTLNNVYSEDRLTGLKATLGINLGHTSEALMASSRIESQVLQWPEGINNSNKLICYRSEQRDLALQLCGWAFEQELDRFIDQLYANKEYSRAAMICVFHLKIFHACNILSSAADNMRDPSMYRITVIALSSFNADRCSSTWRNQRSSANMQIHDPHLRAVFSFLTMEKDNFDAVLKEEGVSLSDRMAFACKYLSETKLADYVAQQIQAAIDGGDLNGLLLTGESQDGIDILQSYMDTSFDVQTVALVAINYFRQELFEDKRIQYWIASYLDHLNSWGLWEKRAELDIKIESIRPSSRSSRTVFLSCNFCGKSVSNALLDEPRPRSTTTSTNRLSSCPSCRKPLPRCSLCLMHMGTMVNMSNGETPTTTPDVPGWQTKPFSKWFSWCQTCRHGGHTEHIMQWFKQNSECPVSSCNCRCFDMDGTKPNTLRDIS
Protein: Tail tube protein (TTP) (Gene product 11) (gp11) (Major tail protein) (MTP) (Q9MCC1)
Organism: Lactococcus phage p2 (Lactococcus lactis bacteriophage p2)
Function: Forms the cylindrical rigid tail tube with a 4 nm wide central channel for DNA ejection. The tube is composed of 31 hexameric rings.
Subcellular location: Virion {ECO:0000269|PubMed:22820334, ECO:0000269|PubMed:24027307}. Note=Constitutes the tail tube. {ECO:0000269|PubMed:22820334, ECO:0000269|PubMed:24027307}.
Interaction partners:
Sequence:
MKLDYNSREIFFGNEALIVADMTKGSNGKPEFTNHKIVTGLVSVGSMEDQAETNSYPADDVPDHGVKKGATLLQGEMVFIQTDQALKEDMLGQQRTENGLGWSPTGNWKTKCVQYLIKGRKRDKVTGEFVDGYRVVVYPHLTPTAEATKESETDSVDGVDPIQWTLAVQATESDIYSNGGKKVPAIEYEIWGEQAKDFAKKMESGLFIMQPDTVLAGAITLVAPVIPNVTTATKGNNDGTIVVPDTLKDSKGGTVKVTSVIKDAHGKVATNGQLAPGVYIVTFSADGYEDVTAGVSVTDHS
Protein: Long neurotoxin MS2 (P86096)
Organism: Micrurus surinamensis (Surinam coral snake)
Function: Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Very weak inhibitor of the endogenous nicotinic acetylcholine receptors (nAChR) in the human rhabdomyosarcoma TE 671 cell line. Not toxic to mice by intraperitoneal injection or to zebrafish by injection at the back of the dorsolateral region.
Subcellular location: Secreted {ECO:0000269|PubMed:18384102}.
Interaction partners:
Sequence:
LTCHTCPYNTCANSETCPAGKNICYQKKWEEHQGERIERRCVANCPKLGSNDKSLLCCRRDDCN
Protein: Atypical chemokine receptor 3a (A0A2R8PYR8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MWEELNFTDSNNNSSRVEAQMCPASFNRSALLNAMCTLYAFIFVVGLAANALVVWVNMRSQRHYHETHMYILNLAVADLCVVATLPVWVSSLAQGGHWAFGQAACKLTHLLFSVNLFASIFFLTCMSVDRYLSVVRFREISHRRGRQVRRLVCAITWLLALFASVPDTYFLRSVKSQYSHVTLCLPVYPEDNPLQWMVGIQLSFVVLGFAIPFPIIAVSYALLANTLASTSTHSPSNGDQDRSVSKKVILMYIVVFIACWAPYHAVLLADALAMLGVLPLGCSSENGLFVALHLTQCLSLLHCCVNPVVYSFAHRHYRYDLMKAFIFKYSTRTGLARLIDGSQGIETEYAMVENNPPTVT
Protein: LBH domain-containing protein 1 (Q9BQE6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALVPGRSKEDGLWTRNSPGSSQHPESPRLPNPLWDRGKIGKVEGHQHIQVSTSSACVWQLAYPPVWPNLPAVPIQDFSQKSHLPSIVVESSEVNEESGDLHLPHEELLLLTDGEEEDAEAFFQDQSEEPGWAWSPQDPRSPLRTFNAGLSWGQDQDEEDACWILEDTACLEATNHCPFWDSTGSRVCRSGFVEYSHLLPPNSFEGAEEEAVQTPAGVESGAASEAPGGRGCDRPRADHAAPPQEAGVQCTCQHYTVREEAQKTPPADPACPEREDSHGSGSPFKASQD
Protein: Specificity protein transcription factor 2 (Q22678)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Probably acts downstream of the Wnt signaling pathway.
Interaction partners:
- Nuclear hormone receptor family member nhr-106
- Acyl_transf_3 domain-containing protein
- Major sperm protein
- L-Fucosyltransferase
Sequence:
MDGAATKFFRPWESHGSYHHSLPSISPPDSPASTSASSSSSSIGANELTTKRRKCERCTCPNCKAIKHGDRGSQHTHLCSVPGCGKTYKKTSHLRAHLRKHTGDRPFVCDWFDCGKRFDRSDQLIRHKRTHTKEYRFACKFCIRQFSRSDHLQQHLTSVHNIVVVD
Protein: Carboxypeptidase Y inhibitor (CPY inhibitor) (CDC25 suppressor 1) (I(C)) (Ic) (Protein DKA1) (Protein NSP1) (P14306)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Specific and potent inhibitor of carboxypeptidase Y.
Subcellular location: Cytoplasm.
Interaction partners:
- Carboxypeptidase Y
- Cerevisin
- Glutamate decarboxylase
- Large ribosomal subunit protein mL40
- Meiotic sister chromatid recombination protein 1
- 6-phosphogluconolactonase 4
- Phosphoglucomutase 2
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL30m
- Large ribosomal subunit protein uL10m
Sequence:
MNQAIDFAQASIDSYKKHGILEDVIHDTSFQPSGILAVEYSSSAPVAMGNTLPTEKARSKPQFQFTFNKQMQKSVPQANAYVPQDDDLFTLVMTDPDAPSKTDHKWSEFCHLVECDLKLLNEATHETSGATEFFASEFNTKGSNTLIEYMGPAPPKGSGPHRYVFLLYKQPKGVDSSKFSKIKDRPNWGYGTPATGVGKWAKENNLQLVASNFFYAETK
Protein: Putative N-acetylated-alpha-linked acidic dipeptidase (NAALADase) (EC 3.4.-.-) (Cell growth-inhibiting gene 26 protein) (Prostate-specific membrane antigen-like protein) (Putative folate hydrolase 1B) (Q9HBA9)
Organism: Homo sapiens (Human)
Function: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:14716746}.
Interaction partners:
Sequence:
MGGSAPPDSSWRGSLKVSYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHETVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEDNSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYNISMKHPQEMKTYSLSFDSLFSAVKNFTEIASKFSERLQDFDKSNPILLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGDVKRQISVAAFTVQAAAETLSEVA
Protein: Putative ATP-dependent helicase IRC3 (EC 3.6.4.-) (Increased recombination centers protein 3) (Q06683)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ATP-dependent DNA helicase HMI1, mitochondrial
- Benzil reductase
- ATP-dependent helicase HRQ1
- ATP-dependent RNA helicase MRH4, mitochondrial
Sequence:
MTSTLATRLSTYSISLILQRIKIIKRCYSAPVLRDYQQDAIDACVNSIRQGTKRIGVSLATGGGKTVIFSNLINQLRQNYFKERQGNFKSLILVHRRELALQATATLKKIFPDLKVHIEMGKYDCDIEDSDVIVASVQTLIRRLHKYDTNSVNLIIIDEAHHSVANSYRSILDHFKASTAETKIPVIGFSATFERADKRALSMVMDKIVYHRGILEMIDDKWLCEAKFTSVKIEADLSDVKSTADDFQLAPLSSLMNTKEINEVILKTYLHKKQEKSLKSTLLFGVDKAHVQSLHKLFKDNGINTDYVTSDTKQIERDNIIQKFKNGETEVLMNCGIFTEGTDMPNIDCILLCRPTKSRSLLIQMIGRGLRLHHSKDHCHIIDFIGASSVGVVSAPTLLGIRSDDIEFDDATVEDLKAIQGEIIAKQQKIDERLRALFQTDEAAMENVTERNSVADWIHSANSVDLTLCSFDSFRNFTQSNNSYPSGKEFDEASEAVKEMELLMNSQYPWVKFASNAWGLPLKGKNHLRIYKEKSEDKLSMVYHLKMYRQLPCFITNKYADYVPKSIIKDANLWNVMSKVEKIINTLNSDLEGQTMQYQAISSKYSKWRQTVPTSKQRDFVFRKLKKVYGESSKDFIRLSLDDVTTYVNTKMTKGDASNLIFASSLAPVYPLKSLLRILEYQKRRSFIK
Protein: Candida glabrata strain CBS138 chromosome H complete sequence (Q6FRI9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Heat shock protein homolog SSE1
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Peptidyl-prolyl cis-trans isomerase D
- Hsp90 chaperone protein kinase-targeting subunit
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MTTADEYKQQGNAAFVAKDYEKAIDLFSKAIEVSETPNHVFYSNRSACYASLKKFPEALNDAEECVKINPTWSKGYNRLGAAHLGLGDLDEAEGSYKKALELDGSNQAAKDGLDQVKRTQESRQGMPDLGLSKIFADPNLIENLKKNPKTSEMMKDPELVAKLIKYKTNPQAMSQDLFTEPRLMTIMATLMGVDLNMPDLSSSNSMPKEPTETPEQSKETPAEQKSEPQAEATKAEPEPMEVDSAGNEETSKKEEAEKEKALGNKAYKARQFDEAIAHYDAAWNLHQDITYLNNRSAAEFEKGDAETALKTLDEAVEKGREMRTDYKLIAKSFARMGNVHHKTNNLKKAIEFYQKSLTEHRTPEILTKLRNTEKELKKQEAEEYINPEKAEEARLEGKDYFTKGDWPNAVKAYTEMIKRAPEDARGYSNRAAALSKLMSFPEAIEDCNKAIEKDPNFIRAYIRKATAQIAVKEFAAAIETLDAARTKDAEVNNSANVREIDQLYVKASQQRFQPASSNETPEQVYERAMKDPEVIAIMQDPVMQSILQQAQQNPAALQEHMKNPDVFKKIQTLIAAGIIRTGP
Protein: Gamma-aminobutyric acid receptor subunit beta (Ionotropic GABA receptor subunit UNC-49B.3) (G5ECD3)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Glutamate decarboxylase 1
- Vesicular GABA transporter
- Moesin/ezrin/radixin homolog 1
- Synaptobrevin-1
- Acetylcholinesterase 1
- Carboxylic ester hydrolase
Sequence:
MARPFTLIVLLSAHLCLHVVVTQDEDSHINTQLLSSVLDRLTNRTTYDKRLRPRYGEKPVDVGITIHVSSISAVSEVDMDFTLDFYMRQTWQDPRLAFGSLDLGLSKEIDSLTVGVDYLDRLWKPDTFFPNEKKSFFHLATTHNSFLRIEGDGTVYTSQRLTVTATCPMDLKLFPMDSQHCKLEIESYGYETKDIDYYWGKKRTDLEITAVKFDTFQLPQFQPTLYFVNTTKAETSSGKYVRLALEVILVRNMGFYTMNIVIPSILIVTISWVSFWLNREASPARVGLGVTTVLTMTTLITTTNNSMPKVSYVKGLDVFLNFCFVMVFASLLEYAIVSYMNKRLVLRREKRRKAAEQQQRNEMPMFNASPKAANNNSYEMTLMSQNSTPAKSYVQADLYFAGHNSSMNPLMEIPENCDCRTIPMMQHPRLVTDGAHTLWPAPFARPKKASKTCCQRWTPAKIDKLSRYGFPLSFSIFNIVYWLYMKYLSLNSSDKIQENDKWQQIH
Protein: Transcription initiation factor IIE subunit alpha (TFIIE-alpha) (Q9P3W1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Transcription initiation factor IIE subunit beta
- Transcription initiation factor IIF subunit alpha
- General transcription and DNA repair factor IIH subunit tfb2
- DNA-directed RNA polymerase II subunit rpb1
- RNA polymerase II transcription factor B subunit 3
- General transcription and DNA repair factor IIH subunit tfb1
- Transcription initiation factor IIF subunit beta
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription and DNA repair factor IIH subunit tfb4
- General transcription and DNA repair factor IIH subunit ssl1
Sequence:
MSNAPEIVQRLIKMIMRAFYETRHIIFMDAILRHSALTDEQTALLMGIPIKECRFIAGKLREDRLLAIQSRTEMKEGQQRQYHTTYFYIDFCSTIDSIKWRMHQLVKTVEDRMRNDFDSKGYVCPFCNKKFSSLDVLSLVTNEGTFACNVCGTELKDDEESAEMMSSQKRLGKLMGQVNGIIDALKRVDEIVVPQNNFQSALEHAVPVSLDTQNLSQQNLSKSNSDVRLSTSSPSITVDFSADKETDEKRERNCDKQVKAAQNILPEWHATSTISGSITRAGAKDAALHSFRTETVNEVQDTKTDITSEKSALDAYYATLRAKQKEESEFMDSENVDDEEDDDFLDVTTATSLQNKSTDYGSVKRKTENLNSDSDIQNKRTKSIEENNSLPPIVSTNGITDGDTEMQESKKNVIINGFNEDDEDDEDEADFEDV
Protein: Interleukin-8 (IL-8) (C-X-C motif chemokine 8) (Chemokine (C-X-C motif) ligand 8) (O62812)
Organism: Equus caballus (Horse)
Function: Chemotactic factor that mediates inflammatory response by attracting neutrophils, basophils, and T-cells to clear pathogens and protect the host from infection. Also plays an important role in neutrophil activation. Released in response to an inflammatory stimulus, exerts its effect by binding to the G-protein-coupled receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes and endothelial cells. G-protein heterotrimer (alpha, beta, gamma subunits) constitutively binds to CXCR1/CXCR2 receptor and activation by IL8 leads to beta and gamma subunits release from Galpha (GNAI2 in neutrophils) and activation of several downstream signaling pathways including PI3K and MAPK pathways.
Subcellular location: Secreted.
Interaction partners:
- C-X-C motif chemokine 6
- C-X-C chemokine receptor type 2
- Interleukin-1 beta
- C-X-C chemokine receptor type 2
- C-X-C motif chemokine
- Nuclear factor NF-kappa-B p105 subunit
- Multifunctional fusion protein
- Atypical chemokine receptor 1
- Transcription factor Jun
- RELA proto-onco, NF-kB subunit
Sequence:
MTSKLAVALLAVFLLSAALCEAAVVSRITAELRCQCIKTHSKPFNPKLIKEMRAIESGPHCENSEIIVKLVNGAEVCLNPHTKWVQIIVQAFLKRAEGQNP
Protein: Coatomer subunit delta (Delta-coat protein) (Delta-COP) (Q93Y22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit alpha-1
- Coatomer subunit gamma
- Coatomer subunit beta-2
- Coatomer subunit beta-1
- Coatomer subunit alpha-2
- Coatomer subunit beta'-3
- Coatomer subunit beta'-2
- Coatomer subunit beta'-1
- Coatomer subunit epsilon-1
- Coatomer subunit epsilon-2
Sequence:
MVVLAAAIVVKSGKVIVSRHYVDMSRIRIEGLLAAFPKLVGMGKQHTYIETENVRYVYQPIEALFLLLVTTKQSNILEDLATLTLLSKLVPEYSMSLDEEGISRASFELIFAFDEVISLGHKESVTVAQVKQYCEMESHEEKLHKLVMQSKINDTKDVMKRKANEIDKSKIEKNKPGGFSSMGSMGSGRLESGFNELSISSGGGGGYGSGSGFGMISDVDPINTKPKDRSRSSVTAPPKSSGMKLGKSGKNQLMESLKAEGEDVIEDVKPTGQSKAAAPPPTDPFTLTVEEKLNVALRRDGGLSSFDMQGTLSLQILNQEDGFVQVQIATGENPEILFKTHPNINRDMFNNENILGLKRPDQPFPTGQGGDGVGLLRWRMQRADESMVPLTINCWPSVSGNETYVSLEYEASSMFDLTNVIISVPLPALREAPSVRQCDGEWRYDPRNSVLEWSILLIDNSNRSGSMEFVVPPVDSSVFFPISVQFAATSTYSGLKVTGMIPLRGGGGATPRFVQRTQLIAQNYQVI
Protein: Ephrin type-A receptor 7 (EC 2.7.10.1) (Developmental kinase 1) (mDK-1) (EPH homology kinase 3) (EHK-3) (Embryonic brain kinase) (EBK) (Q61772)
Organism: Mus musculus (Mouse)
Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 and MAPK3 which are phosphorylated upon activation of EPHA7. Isoform 4 which lacks the kinase domain may regulate isoform 1 adhesive properties.
Subcellular location: Cell membrane {ECO:0000305|PubMed:11089974}; Single-pass type I membrane protein {ECO:0000305|PubMed:11089974}.
Interaction partners:
- Ephrin-A5
- Ephrin-A2
- Ephrin-A1
- Ephrin-A3
- Ephrin-A4
- Tyrosine-protein kinase ABL1
- Ephexin-1
- Ephrin-B2
- Ras GTPase-activating protein 1
- Ephrin-B3
Sequence:
MVVQTRFPSWIILCYIWLLGFAHTGEAQAAKEVLLLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIVENLAVFPDTVTGSEFSSLVEVRGTCVSSAEEEAENSPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRRFYKSSSQDLQCSRCPTHSFSDREGSSRCECEDGYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVQLSWQEPEHPNGVITEYEIKYYEKDQRERTYSTLKTKSTSASINNLKPGTVYVFQIRAVTAAGYGNYSPRLDVATLEEASGKMFEATAVSSEQNPVIIIAVVAVAGTIILVFMVFGFIIGRRHCGYSKADQEGDEELYFHFKFPGTKTYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAGEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEFMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGLSRVIEDDPEAVYTTTGGKIPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKDRAERPKFEQIVGILDKMIRNPSSLKTPLGTCSRPLSPLLDQSTPDFTAFCSVGEWLQAIKMERYKDNFTAAGYNSLESVARMTIDDVMSLGITLVGHQKKIMSSIQTMRAQMLHLHGTGIQV
Protein: Nucleotide-binding oligomerization domain containing 2 (A0A0G2K4Z7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell membrane {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Inflammasome {ECO:0000256|ARBA:ARBA00004110}.
Interaction partners:
Sequence:
MCSQEDFQAQRSQLVALLVSGSLEGFESILDWLLSWDVLSREDYEGLSLPGQPLSHSARRLLDTVCNKGVWGCQKLFEAVQEAQANSHTFELQGCWDVHSLHPTRDLQSHRPAIVRRLCSHVEAILELARDEGFLSQYECEEIRLPIFTSSQRARRLLDLAAVKANGLAAFLLQHVRKLPASLSLPYEGYSLCGSHCDHRLNLIRLFCILAAECQKFTAKLRTMVSAQSRFLSTYDGSENLCLEDIYTENTLELRTEVGTAGALQKSPATLGLEELFGTHGHLNKDADTILVVGEAGSGKSTLLQRLHLLWASGQNFREFLFIFPFSCRQLQCMTKPLSLRTLLFEHCCWPDVGQDDVFQFLLDHPDRVLLTFDGLDEFKFRFTDRERHCSPLDPTSVQTLLFNLLQGNLLKNACKVLTSRPDAVSALLRKFVRTECHLKGFSEEGIKLYLRKHHREPGVADRLIHLIQATSALHGLCHLPVFSWMVSRCHRELLLQNRGFPTTSTDMYLLILQHFLLHASPPDSFPLGLGPGLLQSRLSTLLHLGHLALQGLAMSCYVFSAQQLQAAQVDSEDISLGFLVRAQSVVPGSKAPLEFLHITFQCFFAAFYLAVSADTSAASLKHLFSCGRPGNSLLLRLLPNLCIQGSRVKGGQAALLQKAEPHNLQITAAFLAGLLSQQHRDLLAACQVPERVLLQRQARARSCLAHSLREHFHSIPPAVPGETKSMHAMPGFIWLIRSLYEMQEVQLAREAVRRLDIGHLKLTFCRVGPAECAALAFVLQHLQRPVALQLDHNSVGDVGVEQLLPCLGVCTALYLRDNNISDRGARTLVECALRCEQLQKLALFNNKLTDGCASSVAKLLAHKQNFLSLRVGNNHITAAGAEVLAQGLKSNTSLQFLGFWGNSVGDKGSQALAEVVADHQRLKWLSLVGNNIGSVGAHALALMLEKNKSLEELCLEENHICDEGVYSLAEGLKRNSTLKFLKLSNNGITYRGAEALLQALNRNSTVLEVWLRGNTFSPEEAQTLSSSDARLLL