wanglab/gogpt-training-data huggingface dataset:
Protein: ABC transporter, permease protein, FecCD family (B7JA67)
Organism: Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270))
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Iron compound ABC transporter, ATP-binding protein, putative
- Iron compound ABC transporter, periplasmic iron-binding protein, putative
- Iron compound ABC transporter, periplasmic iron-binding protein, putative
- Uncharacterized protein
- MotA/TolQ/ExbB proton channel family protein
- Uncharacterized protein
- TonB-dependent receptor
- TonB family protein
- TonB-dependent receptor
- Biopolymer transport protein, ExbD/TolR family
Sequence:
MIRIWRLPILFVALLIISGGSLLIGRYPLPISSLWAAVSGANPLLHALLIHVRLPEILAAVMVGAALSVSGSAFQALFMNPLVSPSILGVLSGAAFGAALGIVLGLPWGLAQVISFGFGMLAVFIAIFISRLYPVNPVLMLVLGGIISGALFTALLTMVQYLANPYTQLPTIVYWLMGNLGGVRLSELRIMAIPILLAVLALTAFGKTMNVLSMGDEEARALGVSVHWARMLIIVMATIASALTVSLVGMIAWVGLIVPHIARFMVGPDNRVLIPASALTGGLFLVIADDISRTAFSVEIPLGVVTDLVGIIAFMLVLHRLRKGWTA
Protein: Procollagen C-endopeptidase enhancer 1 (Procollagen COOH-terminal proteinase enhancer 1) (PCPE-1) (Procollagen C-proteinase enhancer 1) (Type 1 procollagen C-proteinase enhancer protein) (Type I procollagen COOH-terminal proteinase enhancer) (Q15113)
Organism: Homo sapiens (Human)
Function: Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity.
Subcellular location: Secreted.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Tolloid-like protein 2
- Bone morphogenetic protein 1
- Collagen alpha-2
- Collagen alpha-2
- Biglycan
- Collagen alpha-1
- Collagen alpha-2
Sequence:
MLPAATASLLGPLLTACALLPFAQGQTPNYTRPVFLCGGDVKGESGYVASEGFPNLYPPNKECIWTITVPEGQTVSLSFRVFDLELHPACRYDALEVFAGSGTSGQRLGRFCGTFRPAPLVAPGNQVTLRMTTDEGTGGRGFLLWYSGRATSGTEHQFCGGRLEKAQGTLTTPNWPESDYPPGISCSWHIIAPPDQVIALTFEKFDLEPDTYCRYDSVSVFNGAVSDDSRRLGKFCGDAVPGSISSEGNELLVQFVSDLSVTADGFSASYKTLPRGTAKEGQGPGPKRGTEPKVKLPPKSQPPEKTEESPSAPDAPTCPKQCRRTGTLQSNFCASSLVVTATVKSMVREPGEGLAVTVSLIGAYKTGGLDLPSPPTGASLKFYVPCKQCPPMKKGVSYLLMGQVEENRGPVLPPESFVVLHRPNQDQILTNLSKRKCPSQPVRAAASQD
Protein: FI11917p (KEAP1) (Q7KSF5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cullin 3, isoform F
- Serine/threonine-protein phosphatase Pgam5, mitochondrial
- Segmentation protein cap'n'collar
- Protein ref
- Glutamate--cysteine ligase
- Rho-related BTB domain containing, isoform B
- Maf-S, isoform B
- Sestrin homolog
- Cullin homolog 1
- GCS light chain
Sequence:
MQTQMHSPMQYETHISDMPNHKGYPCRPEEAEMSNTSESCSISCGGRFGSAHSTLDDHDATDDDMTFCMSNYAKEALKMMYMMRSHGMLTDVVLEVKKELFPAHKVVLSAASPYFKAMFTGGLKESEMSRVQLQGVCPTAMSRILYFMYTGQIRVTEVTVCQLLPAATMFQVPNVIDACCAFLERQLDPTNAIGIAHFAEQHGCVELQKKANVFIERNFTQVCQEEEFLQLSAYQLIALIRRDELNVQEEREVYNAVLKWVKYDEDNRHCKMEHILGAVRCQFLTPNFLKEQMKNCDVLRKVPACREYLAKIFKDLTLHKCPGVKERTPNTTRMIFVAGGFFRHSLDILEAYNVDDMTWTTLANLRIPRSGLGAAFLKGKFYAVGGRNNNIGSSYDSDWVDRYSAVTETWRPCAPMSVPRHRVGVAVMDELMYAVGGSAGMEYHNTVEYYDPDLDRWTLVQPMHAKRLGVGVVVVNRLLYAIGGFDGNERLASVECYHPENNEWSFLPPLQTGRSGAGVAAINQYIYVVGGFDGTRQLATVERYDTENDTWDMVAPIQIARSALSLTPLDEKLYAIGGFDGNNFLSIVEVYDPRTNTWTTGTPLKSGRSGHASAVIYQPACSTTFMDYEDSDAPHPDGSNNGERNAHTPQNTYGSGSPHYPGTASNMQFHTSYGMSGCNNCDSEMDIKPYIPAEHHSFQIPAIRSEELVNPNCPWSRMQERFRRTPPASFTDDERNANDMRHKLKKAQKECLFSTAAKVFHHHIEGRLRKLTSAAT
Protein: MICOS subunit MIC26 (Mitochondrial contact site complex 29 kDa subunit) (Mitochondrial inner membrane organization component of 27 kDa) (Mitochondrial organizing structure protein 2) (MitOS2) (P50087)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Enriched at crista junctions. {ECO:0000269|PubMed:21944719, ECO:0000269|PubMed:21987634, ECO:0000269|PubMed:22009199}.
Interaction partners:
- MICOS complex subunit MIC12
- MICOS complex subunit MIC60
- MICOS complex subunit MIC27
- MICOS complex subunit MIC10
- MICOS complex subunit MIC19
- Sorting assembly machinery 50 kDa subunit
- Mitochondrial import receptor subunit TOM40
- Mitochondrial import receptor subunit TOM22
Sequence:
MTKDFYRQLDPVEEKIVPPENAIVISSEAKEATVNEKEAKQGVLSQRVMKYIGENELVDGISVRDPDYLKRFFNERRKQFSAKWDKVTNKIDDIAGRYYAREESFTSTIASLHTDPNERLIPGLLSILVASMTGSVLARRRTWLLRATMPIILGSCCFAYAMPTTFRNTMGLIHNLEMNTFPHFTERQDRVWKETKRLSTASVQYYYDAKKWLNKDVEKTGNAIKNWTGVNVK
Protein: bZIP transcription factor 53 (AtbZIP53) (Q9LZP8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds DNA to the C-box-like motif (5'-TGCTGACGTCA-3'), ABRE elements, G-box-like motif (5'-CCACGTGGCC-3'), DOF (5'-AAAG-3'), I-box (5'-GATAA-3'), BS1 (5'-AGCGGG-3'), MY3 (5'-CGACG-3'), 5'-CAGTGCGC-3' and 5'-ACTCAT-3' sequence in target gene promoters. DNA-binding and subsequent transcription activation is triggered by heterodimerization with other bZIP proteins (e.g. BZIP1, BZIP10 and BZIP25). Promotes POX1/PRODH1 expression in response to hypoosmolarity stress. Transcriptional activator of seed maturation (MAT) genes (e.g. AT2S2), including seed storage protein (SSP) and late embryogenesis abundant (LEA) genes. Activated by low energy stress both by transcriptional and post-transcriptional mechanisms. Promotes dark-induced senescence and participates in the transcriptional reprogramming of amino acid metabolism during the dark-induced starvation response, especially when heterodimerized with BZIP1, by triggering accumulation of specific proteins including ASN1 and POX1/PRODH1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:16810321}.
Interaction partners:
- Basic leucine zipper 10
- Basic leucine zipper 25
- Basic leucine zipper 63
- bZIP transcription factor 16
- Proline dehydrogenase 1, mitochondrial
- At5g04840
- Basic leucine-zipper 75
- Proline dehydrogenase 2, mitochondrial
- B3 domain-containing transcription factor ABI3
- Asparagine synthetase 1
Sequence:
MGSLQMQTSPESDNDPRYATVTDERKRKRMISNRESARRSRMRKQKQLGDLINEVTLLKNDNAKITEQVDEASKKYIEMESKNNVLRAQASELTDRLRSLNSVLEMVEEISGQALDIPEIPESMQNPWQMPCPMQPIRASADMFDC
Protein: Expressed protein (Late embryogenesis abundant protein, group 6) (Late embryogenesis abundant-like protein) (Q8S8R1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein BIG GRAIN 1-like E
- Copper ion binding protein
- UDP-glycosyltransferase 76C5
- At1g68440/T2E12_1
- Phosphoglycerate mutase family protein
- Leucine-rich repeat
- Glycine-rich protein 3 short isoform
- Insecticidal crystal toxin domain-containing protein
- Protein LNK4
- Staphylococcal-like nuclease CAN2
Sequence:
MEAGKTPPTTTTTTEKKTEQVKDNDLPTDSPYMATGTLEDYKLKAYGAEGHQEPTPGLGGGSTDAPTPSGDAPAATTTDAKAP
Protein: [histone H3]-trimethyl-L-lysine(4) demethylase (EC 1.14.11.67) (A0A0G2K1H0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MELGSDDFLPPPECPVFEPSWAEFRDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRIQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERRILDLYSLSKIVVEEGGYETICKDRRWARVAQRLNYPPGKNIGSLLRSHYERIVYPYEMYQSGANLVQCNTRPFDNEEKDKEYKPHSIPLRQSVQPSKFNSYGRRAKRLQPDPEPTEEDIEKNPELKKLQIYGAGPKMMGLGLMAKDKNLRKKDKEGPECPPTVVVKEELGGDVKMESASPKTFLEGKEELSHSPEPCTKMTMRLRRNHSNAQFIESYVCRMCSRGDEDDKLLLCDGCDDNYHIFCLLPPLPEIPKGVWRCPKCVMAECKRPPEAFGFEQATREYTLQSFGEMADSFKADYFNMPVHMVPTELVEKEFWRLVNSIEEDVTVEYGADIHSKEFGSGFPVSDSKRHLTPEEEEYATSGWNLNVMPVLEQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMKKLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAACPEKLDLNLAAAVHKEMFIMVQEERRLRKALLEKGITEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVCLSHINDLCKCSSSRQYLRYRYTLDELPAMLHKLKVRAESFDTWANKVRVALEVEDGRKRSLEELRALESEARERRFPNSELLQRLKNCLSEAEACVSRALGLVSGQEAGPDRVAGVQMTLAELQDFLGQMNNLPCAMHQIGDVKGILEQVEAYQTEAREALVSQPSSPGLLQSLLERGQQLGVEVPEAQQLQRQVEQARWLDEVKRTLAPSARRGTLAIMRGLLVAGASVAPSPAVDKAQAELQELLTIAERWEEKAHLCLEARQKHPPATLEAIIHEAENIPVHLPNIQSLKEALAKARAWIADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKNSCYTLLEVLCPCADAGSDSTKRSRWMEKELGLYKSDTELLGLSAQDLRDPGSVIVAFKEGEQKEKEGILQLRRTNSAKPSPLASLTTNSSTASICVCGQVPAGVGALQCDLCQDWFHGRCVTVPRLLSSQRSSLTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLPEGEALQCLTERAISWQGRARQVLASEEVTALLGRLAELRQRLQAESKPEESLAYSSDGGDGTGNMPKVQGLLENGDSVTSPEKVATEEGSGKRDLELLSSLLPQLTGPVLELPEATRAPLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLKRVQTLLELEKAERHGSRTRGRALERRRRRKVDRGGEPDDPAREELEPKRVRSSGPEAEEVQEEEELEEETGGEVPPVPFPNNGSPSTQEDQDGLEPVLDAGSDTSAPFSTLTSRLLMSCPQQPSLQQL
Protein: Par-6 family cell polarity regulator gamma b (Par-6 partitioning defective 6-like protein gamma) (Q6TNS1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Protein kinase C iota type
- Cell division control protein 42 homolog
- Par-3 family cell polarity regulator alpha, b.
- Protein kinase C
- Cell division cycle 42-like 2
- Cell division control protein 42 homolog
- Protein PALS1
- Crumbs homolog 3a
- Par-3 family cell polarity regulator.
- Crumbs-like protein 3b.
Sequence:
MNRSFNKSQSLRSLNMNAVEVKSKYGAEFRRFSVDRIKPGKFEEFYKLIMTIHRIANMEVMIGYADIHGDLLPINNDENFSKAVSTAHPLLRIFIQRQEEVDYSNFGTSTLTRKKKAVVTLRNDLNRKRPHIRIGMPQDFRPVSSIIDVDILPESHRRVRLYRYGSDKPLGFYIRDGTSVRVTPHGLEKVPGIFISRMVPGGLAESTGLLAVNDEVLEVNGIEVTGKTLDQVTDMMIANSHNLIVTVKPVNQRNNVVRSSRISGSSGQSSDSSGSVGYPAITVPTGATAISHGYSPEDLESDEESDIVIESNIKRPSRRSNASVASNASRSQTQTTTVTPPSPPTRPQTRPPSTVSTASFHSQPSFNGTVHNSLSYKLHKDLTLQHHPYHSSNPAMRESNGSLHKILSSLRTDPRHSLALPRGGVEEDGTVITL
Protein: Delta-like protein D (DeltaD) (After eight protein) (Q8UWJ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a ligand for Notch receptors and is involved in primary neurogenesis and somitogenesis. Can activate Notch receptors, thereby playing a key role in lateral inhibition, a process that prevents the immediate neighbors of each nascent neural cell from simultaneously embarking on neural differentiation. Required in somite segmentation to keep the oscillations of neighboring presomitic mesoderm cells synchronized.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase mib1
- Neurogenic locus notch homolog protein 1
- Hairy-related 1.
- Notch receptor 3.
- Notch receptor 1b.
- Hairy and enhancer of split-related-7.
- Neurogenic locus notch homolog protein 2 precursor
- Transcription factor HES-5
Sequence:
MGRLMIAVLLCVMISQGFCSGVFELKLQEFLNKKGVTGNANCCKGSAAEGHQCECKTFFRICLKHYQANVSPDPPCTYGGAVTPVLGSNSFQVPESFPDSSFTNPIPFAFGFTWPGTFSLIIEALHTDSTDDLSTENPDRLISRMTTQRHLTVGEEWSQDLQVGGRTELKYSYRFVCDEHYYGEGCSVFCRPRDDTFGHFTCGERGEIICNSGWKGQYCTEPICLPGCDEDHGFCDKPGECKCRVGFSGKYCDDCIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCQNGATCTNTGQGSYTCSCRPGFTGDSCEIEVNECSGSPCRNGGSCTDLENTYSCTCPPGFYGRNCELSAMTCADGPCFNGGHCADNPEGGYFCQCPMGYAGFNCEKKIDHCSSNPCSNDAQCLDLVDSYLCQCPEGFTGTHCEDNIDECATYPCQNGGTCQDGLSDYTCTCPPGYTGKNCTSAVNKCLHNPCHNGATCHEMDNRYVCACIPGYGGRNCQFLLPENPQGQAIVEGADKRYSYEEDDGGFPWTAVCAGIILVLLVLIGGSVFVIYIRLKLQQRSQQIDSHSEIETMNNLTNNRSREKDLSVSIIGATQVKNINKKVDFQSDGDKNGFKSRYSLVDYNLVHELKQEDLGKEDSERSEATKCEPLDSDSEEKHRNHLKSDSSERKRTESLCKDTKYQSVFVLSEEKDECIIATEV
Protein: Protein-L-histidine N-pros-methyltransferase (EC 2.1.1.-) (DORA reverse strand protein) (DREV) (Methyltransferase-like protein 9) (mMETTL9) (Q9EPL4)
Organism: Mus musculus (Mouse)
Function: Protein-histidine N-methyltransferase that specifically catalyzes 1-methylhistidine (pros-methylhistidine) methylation of target proteins. Mediates methylation of proteins with a His-x-His (HxH) motif (where 'x' is preferably a small amino acid). Catalyzes methylation of target proteins such as S100A9, NDUFB3, SLC39A5, SLC39A7, ARMC6 and DNAJB12; 1-methylhistidine modification may affect the binding of zinc and other metals to its target proteins. Constitutes the main methyltransferase for the 1-methylhistidine modification in cell.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H1A3}. Mitochondrion {ECO:0000250|UniProtKB:Q9H1A3}. Note=Colocalizes with membranous compartments such as the endoplasmic reticulum and mitochondria. {ECO:0000250|UniProtKB:Q9H1A3}.
Interaction partners:
- Probable methyltransferase-like protein 25
Sequence:
MRLLAGWLCLSLASVWLARRMWTLRSPLSRSLYVNMTSGPGGPAAAAGGGKDTHQWYVCNREKLCESLQSVFVQSYLDQGTQIFLNNSIEKSGWLFIQLYHSFVSSVFSLFMSRTSINGLLGRGSMFVFSPDQFQRLLRINPDWKTHRLLDLGAGDGEVTKIMSPHFEEIYATELSETMIWQLQKKKYRVLGINEWQNTGFQYDVISCLNLLDRCDQPLTLLKDIRSVLEPTQGRVILALVLPFHPYVENVGGKWEKPSEILEIKGQNWEEQVNSLPEVFRKAGFVVEAFTRLPYLCEGDMYNDYYVLDDAVFVLRPV
Protein: Epididymis luminal protein 2 (V9HW98)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ
Protein: At1g14620/T5E21_15 (Decoy) (Q8L7U3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- 50S ribosomal protein L33
- Small ribosomal subunit protein mS29
- At1g64880
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL34m
- Small ribosomal subunit protein mS33
Sequence:
MPRSSLRLLAKPLLESRRGFCTSSDKIVASVLFERLRVVIPKPDPAVYAFQEFKFNWQQQFRRRYPDEFLDIAKNRAKGEYQMDYVPAPRITEADKNNDRKSLYRALDKKLYLLIFGKPFGATSDKPVWHFPEKVYDSEPTLRKCAESALKSVVGDLTHTYFVGNAPMAHMAIQPTEEMPDLPSYKRFFFKCSVVAASKYDISNCEDFVWVTKDELLEFFPEQAEFFNKMIIS
Protein: Unconventional myosin-VI (Unconventional myosin-6) (A0A8I6ACM8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105}. Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004632}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}.
Interaction partners:
Sequence:
MEDGKPVWAPHPTDGFQMGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNVKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSDTIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIREKLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYVKAGSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSAPSLEYCAELLGLDQDDLRVSLTTRVMLTTAGGTKGTVIKVPLKVEQANSARDALAKTVYSHLFDHVVDRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEVKLVGILDILDEENRLPQPSDQHFTSVVHQKHKDHFRLTIPRKSKLAVHRNLRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRALFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPEKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNLWLVCSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKPEVNRQIKDLEISIDALMAKIKSTMMTREQIQKEYDALVKSSEDLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEMEVKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLAQECRDRELALRIAQNESELISDEAQGDTALRSSSSCPASSKTNGTRPQMTPEQMAKEMSDILSRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYDFAPFLNNSPQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQARPTYATAMLQNLLK
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL) (P22681)
Organism: Homo sapiens (Human)
Function: Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Ubiquitinates SPRY2. Ubiquitinates EGFR. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity).
Subcellular location: Cytoplasm. Cell membrane. Cell projection, cilium {ECO:0000269|PubMed:29237719}. Golgi apparatus {ECO:0000269|PubMed:29237719}. Note=Colocalizes with FGFR2 in lipid rafts at the cell membrane.
Interaction partners:
- Hepatocyte growth factor receptor
- Growth factor receptor-bound protein 2
- Rap guanine nucleotide exchange factor 1
- Proto-oncogene tyrosine-protein kinase Src
- Tyrosine-protein kinase ZAP-70
- Epidermal growth factor receptor
- Protein sprouty homolog 2
- Crk-like protein
- Adapter molecule crk
- SH3 domain-containing kinase-binding protein 1
Sequence:
MAGNVKKSSGAGGGSGSGGSGSGGLIGLMKDAFQPHHHHHHHLSPHPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDTLFMMKELAGAKVERPPSPFSMAPQASLPPVPPRLDLLPQRVCVPSSASALGTASKAASGSLHKDKPLPVPPTLRDLPPPPPPDRPYSVGAESRPQRRPLPCTPGDCPSRDKLPPVPSSRLGDSWLPRPIPKVPVSAPSSSDPWTGRELTNRHSLPFSLPSQMEPRPDVPRLGSTFSLDTSMSMNSSPLVGPECDHPKIKPSSSANAIYSLAARPLPVPKLPPGEQCEGEEDTEYMTPSSRPLRPLDTSQSSRACDCDQQIDSCTYEAMYNIQSQAPSITESSTFGEGNLAAAHANTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGDPTTNVTEGSQVPERPPKPFPRRINSERKAGSCQQGSGPAASAATASPQLSSEIENLMSQGYSYQDIQKALVIAQNNIEMAKNILREFVSISSPAHVAT
Protein: adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Q387P6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- 3', 5'-cyclic nucleotide phosphodiesterase, putative
- Phosphodiesterase
- Phosphodiesterase
Sequence:
MNMLHLDDRNASPAPSGGEHSLPTGGAVCRVAMDTLSVILRAPVALLLLLIVLPQLSVGAEANATAKVLSATWSAYMPQEYVTAINAGFSASLESRNWTVAGSVKVEVVYPRNLDLMPQDFIKEQLELETDQNKIVIVYGPLGDIVTYLALPILMKHNVVAFSPMTGSTFIRQWNPYLYFLRADPAAETLALIRYALCQLRVLRLGFMYLQGVHYGDEEYALTVNVMSQMGYELHGVFTVMSPDGEPAPDGEFREVFERFAAALPQAIIVFGAPEKDTAKFLMMMVAEERIARSYILGPSSVQASLAQMWLHALATAGTSFAPGQLLFTGTNPLAKDSQYIAIKRFQGVMSEYLKTHVSETNITEADYFLTHGTEGELMVYGWLAGEVLTQALSSLEWLKDRTTFVRSLYSQRRYVINDIVIGDYGGTCEGEAAKHGATCECNQGSKAVYVKEMLENGQTTTMESGFTVVKASQCYTESSELQGPLNGLTVFMEDDDTASKAAALWQKGASHLVGKGDLGHSDRFFLHAFNTTIAEAANDLRYEQGERIVTAVFGPVTEAMLDTPNITFIDPLELKPQLNKFRRHVIHLSPTLEQQLYVLSSYLAGDGVGTVDAVICSNEADGIADFLRSSLNEFGVSLRSAVIREDGEGVGKYLPISGTVFVIGLSVPDVREIARKLEERNDLRVIVLFGEFSLLYDMFTTALNNTAGAARLVFATSLPHWGDTETSSKTAQLFHDVEKDSRLWTPLSLLAFATGRLMRVILLHVEEMSPDTLVNFFYADSSIISDDMRYGVFDDTKCDTAEKLSKNDCASNYGATQVSVWSMARALNASIPPLTNPMTPSMSFRDPSEGKLSGASLVGVIIGATFALFLMVALGVVPYFVLRSTRDNNSAPKEPTDPVTIVFTDIESSTAQWAAHPDVMADAVATHHKLIRALISQYECYEVKTVGDSFMIASRNVFMAVQLVRDLQRAFLRHNWGASVFDEYYRSLEQDRALESEGYVPPTARLDPDVYRKLWNGLRVRVGVHTGLCDIRHDEVTKGYDYYGHTSNMAARTESAANGGQILLTRATYLSLSTAEREQLDVTALGAVPLRGVPDPVEMYQVDAVVGRSFAALRLDGEVDLIADSGIINASTSDCASFCELGQSAQAIVAVMRALFGTFTASQRKKLLVPFCERWRVTLPPKTKSVWDDNDCQEVMRRIATKVGHVVDFTAGNTVEPSVDTRRRSSLAFLPLQGLWSGWEGAPRNSPTSSERE
Protein: Large ribosomal subunit protein eL32A (60S ribosomal protein L32-A) (P79015)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL30B
- Large ribosomal subunit protein eL22
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein uL2B
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL39
Sequence:
MAAVNIIKKRTKPFKRHQSDRFKRVGESWRKPRGIDSCVRRRFRGTISMPKIGYGNNKKTRYCMPNGLKAFLVRNVSDVELLLMHNKTYAAEIAGNVSARKRVEIVEKARALGVKVTNAGAKVRSQE
Protein: Flagellar motor switch phosphatase FliY (EC 3.-.-.-) (CheY-P phosphatase FliY) (Flagellar motor switch protein FliY) (P24073)
Organism: Bacillus subtilis (strain 168)
Function: Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The switch is localized at the base of the flagellar motor, in or near the C-ring, attached to the MS-ring. {ECO:0000250}.
Interaction partners:
- Flagellar basal-body rod protein FlgG
- Chemoreceptor glutamine deamidase CheD
- Flagellar secretion chaperone FliS
- Chemotaxis protein CheY
- Flagellar biosynthetic protein FliP
- Probable flagellar assembly protein FliH
- Flagellar biosynthetic protein FliZ
- FlaA locus uncharacterized protein YlxG
- Flagellar hook-associated protein 1
- Flagellar hook-basal body complex protein FliE
Sequence:
MENNRLSQDEIDALLNGTGSTLDEPEIPEVDDLSEMERDAIGEIGNISFGSSATALSTLLNQKVDITTPSVTVIPRSKISDAFPEPYVAIEVNYTEGFSGSNLLVVEQSDAAIIADLMIGGDGKGADPSLGEIHLSAVQEAMNQMMGSAATSMSTVFSKKIDISPPRVELLDVTEEKGTDRIPDDEMLVKVSFNLKVGELIDSSIMQLYPLTFAKDLISSLMNSESAEEEETVQPEVTYEQPKEPVTPEPRIEPKQQQQPPKRQGTAKKAAPVQVSPVEFSAFDPNEAVQAPIHNLDMLLDIPLSITVELGRTKRSVKEILELSAGSIIELDKLAGEPVDILVNQRIVAKGEVVVIEENFGVRVTDILSQAERINNLK
Protein: SD07518p (Signal peptide peptidase (EC 3.4.23.-)) (Q9VPQ7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Membrane-bound transcription factor site-2 protease
- Sp1-like factor for pairing sensitive-silencing, isoform B
- Heat shock protein 83
- Derlin-1
- Protein TRC8 homolog
- Translocon-associated protein subunit beta
- DSec61alpha
- Translocating chain-associated membrane protein
Sequence:
MAEEVIGTVKEVLKGIIENVNAPKNESAPGEKKPSTPEGMAVAYSSLVVMAMLPIIFGSIRSVKLHKLKKSTGEKADTMTKKDAMYFPLIASAALFGLYLFFKIFQKVHINYLLTGYFFVLGVIALAHLLSPVINSLMPAAVPKVPFHILFTKGEGKHKEDIVNYKFSTHDIVCLVISSAIGVWYLLKKHWIANNLFGLAFAINGVEMLHLNNFVTGVILLSGLFFYDIFWVFGTNVMVTVAKSFEAPIKLVFPQDLIENGLNASNFAMLGLGDIVIPGIFIALLLRFDDSKKRKTRIYFYSTLIAYFLGLLATIFVMHVFKHAQPALLYLVPACMGTPLLVALIRGELKVLFAYEDHPEEKPEKKEKKEKDEGVSSSGSKKKESKKGK