wanglab/gogpt-training-data huggingface dataset:
Protein: Heterogeneous nuclear ribonucleoprotein H (hnRNP H) [Cleaved into: Heterogeneous nuclear ribonucleoprotein H, N-terminally processed] (P31943)
Organism: Homo sapiens (Human)
Function: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG).
Subcellular location: Nucleus, nucleoplasm.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein F
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein U
- Serine/arginine-rich splicing factor 1
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Transformer-2 protein homolog beta
- Interleukin enhancer-binding factor 3
Sequence:
MMLGTEGGEGFVVKVRGLPWSCSADEVQRFFSDCKIQNGAQGIRFIYTREGRPSGEAFVELESEDEVKLALKKDRETMGHRYVEVFKSNNVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGITLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYNGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSTFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEDAVAAMSKDKANMQHRYVELFLNSTAGASGGAYEHRYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSGGYGGGYGGQSSMSGYDQVLQENSSDFQSNIA
Protein: Putative HTH-type transcriptional regulator YhjB (P37640)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Transcriptional regulatory protein UhpA
- Nitrate/nitrite response regulator protein NarP
- Fimbriae Z protein
- DNA-binding transcriptional activator EvgA
- Transcriptional regulatory protein RcsB
- Response regulator UvrY
Sequence:
MQIVMFDRQSIFIHGMKISLQQRIPGVSIQGASQADELWQKLESYPEALVMLDGDQDGEFCYWLLQKTVVQFPEVKVLITATDCNKRWLQEVIHFNVLAIVPRDSTVETFALAVNSAAMGMMFLPGDWRTTPEKDIKDLKSLSARQREILTMLAAGESNKEIGRALNISTGTVKAHLESLYRRLEVKNRTQAAMMLNISS
Protein: DNA topoisomerase 3-beta-1 (EC 5.6.2.1) (DNA topoisomerase III beta-1) (Q9Z321)
Organism: Mus musculus (Mouse)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Possesses negatively supercoiled DNA relaxing activity.
Interaction partners:
- Fanconi anemia group M protein homolog
- Tudor domain-containing protein 3
- RecQ-mediated genome instability protein 1
- Replication protein A 14 kDa subunit
- RecQ-like DNA helicase BLM
- Replication protein A 70 kDa DNA-binding subunit
- Replication protein A 32 kDa subunit
- RecQ-mediated genome instability protein 2
- DNA topoisomerase 3-alpha
- Structure-specific endonuclease subunit MUS81
Sequence:
MKTVLMVAEKPSLAQSIAKILSRGNMSSHKGLNGACSVHKYTGTFAGQPVHFKMTSVCGHVMTLDFLGKYNKWDKVDPAELFSQAPTEKKEANPKLNMVKFLQVEGRGCDYVVLWLDCDKEGENICFEVLDAVLPVMNNAHNGEKTVFRARFSSITDTDICNAMTRLSEPDHNEALSVDARQELDLRIGCAFTRFQTKYFQGKYGDLDSSLISFGPCQTPTLGFCVERHDKIQSFKPETYWVLQAKVHTDKEESLLLDWDRVRVFDWEIAQMFLNMTKLEKEAWVEATSRKEKAKQRPLALNTVEMLRVASSALGMGPQHAMQIAERLYTQGYISYPRTETTHYPENFDLKGSLRQQANHPYWADSVKQLLAEGINRPRKGHDAGDHPPITPMKSATEAELGGDAWRLYEYITRHFIATVSHDCKYLQSTISFRIGPEHFTCMGKTVISPGFTEIMPWQSVPLEESLPTCQKGDTFTVGEVKMLEKQTSPPDYLTEAELITLMEKHGIGTDASIPVHINNICQRNYVTVESGRRLKPTNLGIVLVHGYYKIDAELVLPTIRSAVEKQLNLIAQGKADYHQVLGHTLDIFKRKFHYFVDSIAGMDELMEVSFSPLAATGKPLSRCGKCHRFMKYIQAKPSRLHCSHCDETYTLPQNGTIKLYKELRCPLDDFELVLWSSGSRGKSYPLCPYCYNHPPFRDMKKGMGCNECTHPTCQHSLSMLGIGQCVECENGVLVLDPTSGPKWKVACNTCNVVAHCFENAHRVRVSADTCNTCEAALLDVDFNKAKSPLPGNETQHTGCIFCDPVFQELVELKHAASCHPMHRGGPGRRQGRGRGRGRRPPGKPNPRRPKDKMSALAAYFV
Protein: EF-hand domain family member A1 isoform 2 (A0A0S2Z6B0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
Sequence:
MAAAAGSCARVAAWGGKLRRGLAVSRQAVRSPGPLAAAVAGAALAGAGAAWHHSRVSVAARDGSFTVSAQKNVEHGIIYIGKPSLRKQRFMQFSSLEHEGEYYMTPRDFLFSVMFEQMEHSSEN
Protein: Solute carrier family 2, facilitated glucose transporter member 5 (Fructose transporter) (Glucose transporter type 5, small intestine) (GLUT-5) (P22732)
Organism: Homo sapiens (Human)
Function: Functions as a fructose transporter that has only low activity with other monosaccharides. Can mediate the uptake of 2-deoxyglucose, but with low efficiency. Essential for fructose uptake in the small intestine (By similarity). Plays a role in the regulation of salt uptake and blood pressure in response to dietary fructose (By similarity). Required for the development of high blood pressure in response to high dietary fructose intake (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q9WV38}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9WV38}. Cell membrane {ECO:0000269|PubMed:1695905, ECO:0000269|PubMed:28083649, ECO:0000269|PubMed:7619085, ECO:0000269|PubMed:8333543}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9WV38}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P43427}. Note=Localized on the apical membrane of jejunum villi, but also on lateral plasma membranes of the villi. Transport to the cell membrane is dependent on RAB11A. {ECO:0000250|UniProtKB:Q9WV38}.
Interaction partners:
- Carbonic anhydrase 6
- Sodium/glucose cotransporter 1
- Ketohexokinase
- Carbonic anhydrase 3
- Alpha-enolase
- Solute carrier family 22 member 12
Sequence:
MEQQDQSMKEGRLTLVLALATLIAAFGSSFQYGYNVAAVNSPALLMQQFYNETYYGRTGEFMEDFPLTLLWSVTVSMFPFGGFIGSLLVGPLVNKFGRKGALLFNNIFSIVPAILMGCSRVATSFELIIISRLLVGICAGVSSNVVPMYLGELAPKNLRGALGVVPQLFITVGILVAQIFGLRNLLANVDGWPILLGLTGVPAALQLLLLPFFPESPRYLLIQKKDEAAAKKALQTLRGWDSVDREVAEIRQEDEAEKAAGFISVLKLFRMRSLRWQLLSIIVLMGGQQLSGVNAIYYYADQIYLSAGVPEEHVQYVTAGTGAVNVVMTFCAVFVVELLGRRLLLLLGFSICLIACCVLTAALALQDTVSWMPYISIVCVISYVIGHALGPSPIPALLITEIFLQSSRPSAFMVGGSVHWLSNFTVGLIFPFIQEGLGPYSFIVFAVICLLTTIYIFLIVPETKAKTFIEINQIFTKMNKVSEVYPEKEELKELPPVTSEQ
Protein: Exosome complex component rrp43 (Ribosomal RNA-processing protein 43) (Q10205)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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 cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. 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. ski6 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Exosome complex exonuclease dis3
- Exosome complex component rrp4
- Exosome complex exonuclease rrp6
- Exosome complex component rrp42
- Uncharacterized GTP-binding protein P8A3.05
- Exosome complex component rrp40
- Exosome complex protein C1739.07
- Exosome complex component rrp45
- Exosome complex component rrp46
- Exosome complex component mtr3
Sequence:
MKTVSGVKQLSFTPSIFKKITPEQYLSHLLNQDVRSDGRSVSEFREIVINDNCISTANGSAIIRAGENVFVCGIKAEIAEPFENSPNEGWIVPNLELSPLCSSKFKPGPPSDLAQVVSQELHQTLQQSNLINLQSLCIFEKKAAWVLYADIICLNYDGSAFDYAWAALFAALKTVKLPTAVWDEDLERVICASTLTRPVQLSTEVRSFSWSVFDDKLLADPTDEEEDLSTEFLTIMLNSSKNIVKIIKLGGTHIQPLLLKKCIEVARSKF
Protein: Glycophorin (A0A087WU29)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLDTSFITPQEIVSISALSTTEVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ
Protein: RING-type domain-containing protein (A7TJH8)
Organism: Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus)
Interaction partners:
- Uncharacterized protein
- Mitogen-activated protein kinase
- Guanine nucleotide-binding protein subunit gamma
- mitogen-activated protein kinase kinase
- Serine/threonine-protein kinase STE11
- Mitogen-activated protein kinase
Sequence:
MYSNHDEILNQLTNIGGGYQYSPVKTPVAENSSEFENSKKSTPSPFSRNKSWTSKLAKFQLSNSRKKKTPTQSPASISSQELNYSEKTNQVPSITPIITPSSQYPTRISSLPRPNSMVFHQNSRKVSSNSAHSNDSNKSQTKKNVPKQQMPFQYTKLTNLAKKSFLNESCTLCEESISNRTNGERVIQLECGHVTHQECLTISFGNSNNYDKTDIYSLFPVCAKCKVERFKSNRCIPNSDEIKDRLVSDFLIGKNSITAQSLNQLDPEMINELMSPLPSPIQEVERKSMYQSVGSPVSSFESHRSVSPINRGGMSLMNPPSGPRNRSNFGKSYSRIGSTIVASSSIHSSADDHESIFSEVASSNFDPGNDEEDKIPLPLIRSYFVEMLVNNFEGEITKWTCDDNFGLLRLVDKLSVSENGSDYTNCQCFLFEKSMVIAEINEENNAKPNNDSIFLGTSLINLKIYICTTGIKVETRNSSVLKVTINNGQNSKPSSLYLTENIDSISSKVIQKWISGLLDSELLFNESNFTSTLSLPTVIQNLGDEEEKSTFVGLISPNKIVEVARLENNRESTIIRRGITVFSGIENGTNMDTLQTMMTSVSSILSLKRERPEGIVIILQLDFRKLKDDSYIIIYNSLQALVTKYPNLIYCTVDADGFVVQYGQASKDILNLQSIYKMNKPNAGIKFSPTWLKNTIYPLGITSSLGIAILSNGSMEEARSCLLMDYKIFASPGRRHANELKIKVGYLNSDYSDKITELVEIGTWAFMLEALCYSFSLSFEDDDDDEDEDDAGDDRDYYDDYSSINSDEKSITTLLIHTPLDGTFPTPVFTEDDRDNNSIVNSLQIDYT
Protein: Slc5a5 protein (Sodium/iodide cotransporter) (Solute carrier family 5 member 5) (A4IG60)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Iodotyrosine deiodinase
- Thyrotropin receptor
- Thyroglobulin.
- Forkhead box E1.
- Paired box protein Pax-8
- Pendrin
- Thyroid-stimulating hormone subunit beta a.
- Thyrotropin receptor
- Dual oxidase 2.
- UDP-glucuronosyltransferase
Sequence:
MAMDSDRPPGFCLVDYAVFAAMLGVSVGIGLFQSLRKTPGRSKVDSFFTGGRGFSAVPVGLSLCASFMSAVQVLGVPSETYLYGFKFLYMCLGQGLNSLMTAVLFVPVFYRLKITSSSQYLGMRFGRGMQLLGSLQFIVATLLYTGIVIFAPAVILNQATGLNMWASLFSTGLICTFYTTVGGMKAVIWTDVFQIVVMLSGFIAVFIQGTILAGGPARVLEIANNGSRINFNDFAIDPQRRYSFWSFTVGGTMVWLSMYGANQAQVQRYISCRTEKQAQLALLVNQVGLCLIVSSAATCGIVMFALYSNCDPLKIGRISAPDQYMPYLVLDIFRNHPGFPGLFLACAYSGTLSTVSTSINAMAAVTMEDVMKPWLITISQRKQLMLSRALSLFYGLGCITMAALSSLLDWGVLQGSFTVMGVVNGPLLGAFALGMFVPATNKPGVFSGVAVGFCLSLWLAVGSTIYPPSPQIMGVLPTSAGQCLTTNATLNTTASVLASSVPLDYSFQNIYSISYLYFGALSTSAVVLVGVVVSYITGPTKKDSISPGLLRWNLEQKPCDASCHILNETITLNPTEILLTPKELFPIAADKQDILLTKGEI
Protein: Cytochrome P450 2U1 (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) (Q7Z449)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of arachidonic acid and its conjugates. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Acts as an omega and omega-1 hydroxylase for arachidonic acid and possibly for other long chain fatty acids. May modulate the arachidonic acid signaling pathway and play a role in other fatty acid signaling processes. May down-regulate the biological activities of N-arachidonoyl-serotonin, an endocannabinoid that has anti-nociceptive effects through inhibition of fatty acid amide hydrolase FAAH, TRPV1 receptor and T-type calcium channels. Catalyzes C-2 oxidation of the indole ring of N-arachidonoyl-serotonin forming a less active product 2-oxo-N-arachidonoyl-serotonin.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14660610}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:14660610}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:23176821}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 4A11
- Cytochrome P450 4F3
- Cytochrome P450 4A22
- Cytochrome P450 4F8
- Cytochrome P450 4F2
- Cytochrome P450 2J2))
- Cytochrome P450 2E1
- Cytochrome P450 2B6
- Cytochrome P450 2C9
- Cytochrome P450 2C8
Sequence:
MSSPGPSQPPAEDPPWPARLLRAPLGLLRLDPSGGALLLCGLVALLGWSWLRRRRARGIPPGPTPWPLVGNFGHVLLPPFLRRRSWLSSRTRAAGIDPSVIGPQVLLAHLARVYGSIFSFFIGHYLVVVLSDFHSVREALVQQAEVFSDRPRVPLISIVTKEKGVVFAHYGPVWRQQRKFSHSTLRHFGLGKLSLEPKIIEEFKYVKAEMQKHGEDPFCPFSIISNAVSNIICSLCFGQRFDYTNSEFKKMLGFMSRGLEICLNSQVLLVNICPWLYYLPFGPFKELRQIEKDITSFLKKIIKDHQESLDRENPQDFIDMYLLHMEEERKNNSNSSFDEEYLFYIIGDLFIAGTDTTTNSLLWCLLYMSLNPDVQEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAPHPFNITISRR
Protein: Ubiquinone biosynthesis accessory factor UbiK (Q46868)
Organism: Escherichia coli (strain K12)
Function: Required for efficient ubiquinone (coenzyme Q) biosynthesis under aerobic conditions. UbiK is probably an accessory factor of Ubi enzymes and facilitates ubiquinone biosynthesis by acting as an assembly factor, a targeting factor, or both. Dispensable for ubiquinone biosynthesis under anaerobiosis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02216, ECO:0000269|PubMed:30686758}.
Interaction partners:
- Ubiquinone biosynthesis accessory factor UbiJ
- 2-octaprenylphenol hydroxylase
- 3-demethoxyubiquinol 3-hydroxylase
- 2-octaprenyl-6-methoxyphenol hydroxylase
- Ubiquinone biosynthesis O-methyltransferase
- Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE
Sequence:
MIDPKKIEQIARQVHESMPKGIREFGEDVEKKIRQTLQAQLTRLDLVSREEFDVQTQVLLRTREKLALLEQRISELENRSTEIKKQPDPETLPPTL
Protein: Autophagy protein 5 (F1RDC0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Preautophagosomal structure membrane {ECO:0000256|ARBA:ARBA00004623, ECO:0000256|RuleBase:RU361202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004623, ECO:0000256|RuleBase:RU361202}.
Interaction partners:
- Ubiquitin-like protein ATG12
- Ubiquitin-like modifier-activating enzyme ATG7
- ATG16 autophagy-related 16-like 1
- Ubiquitin-like-conjugating enzyme ATG3
- Beclin-1
- GABA
- ATG16 autophagy-related 16-like 2
- Tectonin beta-propeller repeat-containing 1b
- WD repeat domain phosphoinositide-interacting protein 2 isoform X1
- ATG10 autophagy-related 10 homolog
Sequence:
MIMADDKDVLRDVWFGRIPACFTLSPDETTEREAEPYYLLLPRVSYLTLVTDKVKKHFLKVMKAEDVEEMWFEHEGTPLKWHYPIGVLFDLHASNSALPWNITVHFKNFPEQDLLHCSTNSVIEAHFMSCIKEADALKHKGQVINDMQKKDHKQLWMGLQNDKFDQFWAMNRKLMEYPTEEGGFRYIPFRIYQTMSDRPFIQTLFRPVSSEGQALTLGDLLKELFPAAIEDEPKKFQVMIHGIEPLLETPIQWLSEHLSHPDNFLHISIIPAPSD
Protein: Chaperone DnaJ-domain superfamily protein (F4J794)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- Chaperone DnaJ-domain superfamily protein
- At3g17830
- Chaperone DnaJ-domain superfamily protein
- At3g13310
- NAD
- At2g17880
- Chaperone protein dnaJ A6, chloroplastic
- At1g77930
Sequence:
MECLRVFASVPKISFFSNSRYSTSQRFIPSCRGKNREDPLSSSSPYSILGVEPSCSSSELKAAFRAKVKQYHPDVNKDGSNSDIMIRRIIQAYEMLTNYSRSEIIEGECLDPFDHPECEALDVFVNEVLCVGKRCSYPCFETASHVFSCDSSGTARAMSQGHGEDYRVQSAVNQCPRNCIHYVTPSQRIILEELLDSVVDKPYDCSAEAEFLYALIVKAKFENNRYQKPKKKQPESSGKHVDWF
Protein: Voltage-dependent L-type calcium channel subunit beta-2 (CAB2) (Calcium channel voltage-dependent subunit beta 2) (Q8CC27)
Organism: Mus musculus (Mouse)
Function: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.
Subcellular location: Cell membrane, sarcolemma {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent L-type calcium channel subunit beta-4
Sequence:
MVQSDTSKSPPVAAVAQESQMELLESAAPAGALGAQSYGKGARRKNRFKGSDGSTSSDTTSNSFVRQGSADSYTSRPSDSDVSLEEDREAVRREAERQAQAQLEKAKTKPVAFAVRTNVRYSAAQEDDVPVPGMAISFEAKDFLHVKEKFNNDWWIGRLVKEGCEIGFIPSPVKLENMRLQHEQRAKQGKFYSSKSGGNSSSSLGDIVPSSRKSTPPSSAIDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPFFKKTEHTPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFEGRISITRVTADISLAKRSVLNNPSKHAIIERSNTRSSLAEVQSEIERIFELARTLQLVVLDADTINHPAQLSKTSLAPIIVYVKISSPKVLQRLIKSRGKSQAKHLNVQMVAADKLAQCPPQESFDVILDENQLEDACEHLADYLEAYWKATHPPSGNLPNPLLSRTLASSTLPLSPTLASNSQGSQGDQRPDRSAPRSASQAEEEPCLEPVKKSQHRSSSATHQNHRSGTGRGLSRQETFDSETQESRDSAYVEPKEDYSHEHVDRYVPHREHNHREETHSSNGHRHRESRHRSRDMGRDQDHNECIKQRSRHKSKDRYCDKEGEVISKRRNEAGEWNRDVYIRQ
Protein: Protein kinase superfamily protein (F4HQQ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MLFPITNYEPSRRNLLASVPLLFCQGASTKYDAKDIGSLGSKASSVSVRPSPRTEGEILQSPNLKSFSFAELKSATRNFRPDSVLGEGGFGCVFKGWIDEKSLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEWAKPYLVNKRKIFRVIDNRLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLEHIQSLNAAIGGNMDKTDRRMRRRSDSVVSKKVNAGFARQTAVGSTVVAYPRPSASPLYV
Protein: Potassium voltage-gated channel protein eag (Ether-a-go-go protein) (Q02280)
Organism: Drosophila melanogaster (Fruit fly)
Function: Structural component of a potassium channel. Mediates the potassium permeability of membranes; potassium current is regulated by CaMKII and CASK. Has a role in growth of the perineurial glial layer of the larval peripheral nerve.
Subcellular location: Membrane {ECO:0000269|PubMed:15901771}; Multi-pass membrane protein {ECO:0000269|PubMed:15901771}. Note=Eag recruits CASK to the plasma membrane.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type II alpha chain
- Potassium voltage-gated channel protein Shal
- Potassium voltage-gated channel protein Shab
- Hyperkinetic, isoform M
- KCNQ potassium channel, isoform F
- Calmodulin
- Potassium voltage-gated channel protein Shaker
- Calcium-activated potassium channel slowpoke
- Shaw-like, isoform C
Sequence:
MPGGRRGLVAPQNTFLENIIRRSNSQPDSSFLLANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRYVCGFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNLQCGCALSQFGKAQTQETPLWLLLQVAPIRNERDLVVLFLLTFRDITALKQPIDSEDTKGVLGLSKFAKLARSVTRSRQFSAHLPTLKDPTKQSNLAHMMSLSADIMPQYRQEAPKTPPHILLHYCAFKAIWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFVGPGGEVVSDPKVIRMNYLKSWFIIDLLSCLPYDVFNAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLDRYLEYGAAMLILLLCFYMLVAHWLACIWYSIGRSDADNGIQYSWLWKLANVTQSPYSYIWSNDTGPELVNGPSRKSMYVTALYFTMTCMTSVGFGNVAAETDNEKVFTICMMIIAALLYATIFGHVTTIIQQMTSATAKYHDMLNNVREFMKLHEVPKALSERVMDYVVSTWAMTKGLDTEKVLNYCPKDMKADICVHLNRKVFNEHPAFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDEVVAILGKGDVFGDQFWKDSAVGQSAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSFARNLVLTYNLRHRLIFRKVADVKREKELAERRKNEPQLPQNQDHLVRKIFSKFRRTPQVQAGSKELVGGSGQSDVEKGDGEVERTKVFPKAPKLQASQATLARQDTIDEGGEVDSSPPSRDSRVVIEGAAVSSATVGPSPPVATTSSAAAGAGVSGGPGSGGTVVAIVTKADRNLALERERQIEMASSRATTSDTYDTGLRETPPTLAQRDLIATVLDMKVDVRLELQRMQQRIGRIEDLLGELVKRLAPGAGSGGNAPDNSSGQTTPGDEICAGCGAGGGGTPTTQAPPTSAVTSPVDTVITISSPGASGSGSGTGAGAGSAVAGAGGAGLLNPGATVVSSAGGNGLGPLMLKKRRSKSRKAPAPPKQTLASTAGTATAAPAGVAGSGMTSSAPASADQQQQHQSTADQSPTTPGAELLHLRLLEEDFTAAQLPSTSSGGAGGGGGSGSGATPTTPPPTTAGGSGSGTPTSTTATTTPTGSGTATRGKLDFL
Protein: Contactin-2 (Axonin-1) (P28685)
Organism: Gallus gallus (Chicken)
Function: Axon-associated cell adhesion molecule (AxCAM) which promotes neurite outgrowth by interaction with the AxCAM L1 (G4) of neuritic membrane. Contributes to the organization of axonal domains at nodes of Ranvier (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor. Note=Attached to the neuronal membrane by a GPI-anchor.
Interaction partners:
- Neuronal cell adhesion molecule
- Contactin associated protein like 2.
- Neural cell adhesion molecule 1
- Receptor-type tyrosine-protein phosphatase gamma
Sequence:
MGGTAAFICTSLAVIICVVWCQAQSGMRSYGPVFEEQPAHTLFPEGSAEEKVTLTCRARANPPATYRWKMNGTELKMGPDSRYRLVAGDLVISNPVKAKDAGSYQCVATNARGTVVSREASLRFGFLQEFSAEERDPVKITEGWGVMFTCSPPPHYPALSYRWLLNEFPNFIPADGRRFVSQTTGNLYIAKTEASDLGNYSCFATSHIDFITKSVFSKFSQLSLAAEDARQYAPSIKAKFPADTYALTGQMVTLECFAFGNPVPQIKWRKLDGSQTSKWLSSEPLLHIQNVDFEDEGTYECEAENIKGRDTYQGRIIIHAQPDWLDVITDTEADIGSDLRWSCVASGKPRPAVRWLRDGQPLASQNRIEVSGGELRFSKLVLEDSGMYQCVAENKHGTVYASAELTVQALAPDFRLNPVKRLIPAARSGKVIIPCQPRAAPKATVLWTKGTELLTNSSRVTITADGTLILQNISKSDEGKYTCFAENFMGKANSTGILSVRDATKITLAPSSADINVGENLTLQCHASHDPTMDLTFTWSLDDFPIDLDKSEGHYRRASVKEAVGDLAIVNAQLKHSGRYTCTAQTVVDSTSESATLTVRGPPGPPGGVVVRDIGDTTVQLSWSRGFDNHSPIARYSIEARTLLSNKWKQMRTNPVNIEGNAETAQVVNLIPWMDYEFRVLASNILGVGEPSLPSSKIRTKEAAPTVAPSGLGGGGGAPNELIINWTPTLRDYQNGDGFGYILSFRKKGTQGWLTARVPHAESLHYVYRNESIGPYTPFEVKIKAYNRKGEGPESLTAIVYSAEEEPKVAPFRVTAKAVLSSEMDVSWEPVEQGDMTGVLLGYEIRYWKDGDKEEAADRVRTAGLVTSAHVTGLNPNTKYHVSVRAYNRAGAGPPSPSTNITTTKPPPRRPPGNISWTLTGSTVTIKWDPVVAQADESAVTGYKMLYRQDSHSAPTLYLASKSRIDIPVPEDFTHAFVQIRVTGPGGDGTPAEVHIVRNSGTSMMVEDSVTRPVPHAAIITTNSLAMVALIRYLEL