wanglab/gogpt-training-data huggingface dataset:
Protein: Cytotoxic T-lymphocyte protein 4 (Cytotoxic T-lymphocyte-associated antigen 4) (G3V7D2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MARLGVQRYKTHLQLPSRTWPFGVLLSLLFIPIFSEAIQVTQPSVVLASSHGVASFPCEYASSHNTDEVRVTVLRQTNDQVTEVCATTFTVKNTLGFLDDPFCSGTFNESRVNLTIQGLRAADTGLYFCKVELMYPPPYFVGMGNGTQIYVIAKEKKSSYNRGLCENAPNRARM
Protein: Meiotically up-regulated gene 115 protein (Q10262)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MRKPCYAVYHPALRLKCLVRKGLGKIKGDTDMCDKQQLKKKEKEKQRAQKVACGPRDPPCTFSRSYTDQKRKEIHLGSTEWGLKESFTLTRGPNRRGNVGKGVKRPMVNKKLGQLELTSLDLRWQKEGKGN
Protein: Root phototropism protein 3 (BTB/POZ domain-containing protein RPT3) (Non-phototropic hypocotyl protein 3) (Q9FMF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Signal transducer of the phototropic response and photo-induced movements. Involved in the phot1 pathway under low blue light (LBL) fluence rate and in the phot2 pathway under higher fluence rate of blue light (HBL). Necessary for root and hypocotyl phototropisms, but not for the regulation of stomata opening. Not involved in chloroplast accumulation and translocation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10542152, ECO:0000269|PubMed:16777956}; Peripheral membrane protein {ECO:0000269|PubMed:10542152, ECO:0000269|PubMed:16777956}.
Interaction partners:
- Phototropin-1
- Protein PHYTOCHROME KINASE SUBSTRATE 2
- Protein PHYTOCHROME KINASE SUBSTRATE 3
- Aspartic proteinase A2
- Protein PHYTOCHROME KINASE SUBSTRATE 4
- Protein PHYTOCHROME KINASE SUBSTRATE 1
Sequence:
MMWESESDGGVGVGGGGGREYGDGVLSSNKHGGVKTDGFELRGQSWFVATDIPSDLLVKIGDMNFHLHKYPLLSRSGKMNRLIYESRDPDPTILILDDLPGGPEAFELASKFCYGVPVDLTATNISGLRCAAEYLEMTEDLEEGNLIFKTEAFLSYVVLSSWRDSILVLKSCEKLSPWAENLQIVRRCSESIAWKACSNPKGIRWAYTGKAPSPSTTNFAGSSPRWNESKDSSFYCSPSRNTNSQPVPPDWWFEDVSILRIDHFVRVITAIKVKGMRFELLGAVIMHYAGKWLPGLIKEGGVAIAPAMSSAIGGGLGLGGDEMSISCGSNSSGGSSGPDWKGGLHMVLSAGKTNGHQDSVACLAGLGISPKDQRMIVESLISIIPPQKDSVTCSFLLRLLRAANMLKVAPALITELEKRVGMQFEQATLQDLLIPGYNNKGETMYDVDLVQRLLEHFLVQEQTEGSSPSRMSPSPSQSMYADIPRGNNNNGGGGGGNNQNAKMRVARLVDSYLTEVARDRNLPLTKFQVLAEALPESARTCDDGLYRAIDSYLKAHPTLSEHERKRLCRVMDCQKLSMDACMHAAQNERLPLRVVVQVLFSEQVKISNALANTSLKESTTLGEAMGTYQPMIPNRKTLIEATPQSFQEGWAAAKKDINTLKFELETVKTKYVELQNEMEVMQRQFEKTGKVKNTPSSSAWTSGWKKLSKLTKMSGQESHDISSGGEQAGVDHPPPRKPRRWRNSIS
Protein: Histocompatibility 2, Q region locus 2 (MHC class I antigen) (Q4KN81)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Beta-2-microglobulin
- H-2 class II histocompatibility antigen, E-B beta chain
- Class II histocompatibility antigen, M alpha chain
- Tapasin
- H-2 class II histocompatibility antigen gamma chain
- H2-O alpha
- H-2 class II histocompatibility antigen, A-B alpha chain
- H-2 class I histocompatibility antigen, Q7 alpha chain
- Class II histocompatibility antigen, M beta 1 chain
- H-2 class I histocompatibility antigen, K-B alpha chain
Sequence:
MALRRLLLLLVAALKLTETRAGSHSLRYFTTAVSRPGLGEPRFIIVGYVDDTQFVRFDSDAENPRMEPRAPWMEQEGPEYWERNTQVSKENEQSFRVSLGTALSYYNQSKGGSHTLQWLVGCDLGPDGSLLRGYEQSAYDGRDYLALNEDLITWTAADLAALKTRSKLEQAGLAEKRRAYLEVDCLTWLRRYLELGKETLLHTDPPKAHVTHHPSSQGDVTLRCWALGFYPADITLTWQLNGEDLTQDMELVETRPSGDGTFQKWASVMVPFGEEPRYTCHVEHEGLPEPLTLRWEPPPSTDSYMVIIAVLVVLGAVIIIGAVVAFVMKRGRNTGGKVRDYAQDPGRDSPQSSDISLLEL
Protein: Calmodulin-3 (P0DP25)
Organism: Homo sapiens (Human)
Function: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules.
Interaction partners:
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: Rho-related GTP-binding protein RhoV (Rho family GTPase Chp) (Q9Z1Y0)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the control of the actin cytoskeleton via activation of the JNK pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}; Lipid-anchor {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}; Cytoplasmic side {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}. Endosome membrane {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}; Lipid-anchor {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}; Cytoplasmic side {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}. Note=Treatment with TNF activates endosomal but not plasma membrane RHOV. {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Intersectin 2
- Intersectin-1
- Rho guanine nucleotide exchange factor 7
- non-specific serine/threonine protein kinase
- Unconventional myosin-IXa
- NCK adaptor protein 1.
- Partitioning defective 6 homolog alpha
- Ras GTPase-activating-like protein IQGAP1
- Par-6 family cell polarity regulator beta
Sequence:
MPPRELSEAEPPPLPASTPPPRRRSAPPELGIKCVLVGDGAVGKSSLIVSYTCNGYPSRYRPTALDTFSVQVLVDGAPVRIELWDTAGQEDFDRLRSLCYPDTDVFLACFSVVQPSSFQNITEKWLPEIRTHNPQAPVLLVGTQADLRDDVNVLIQLDQGGREGPVPEPQAQGLAEKIRACCYLECSALTQKNLKEVFDSAILSAIEHKARLEKKLNAKGVRTLSRCRWKKFFCFV
Protein: Exocyst complex component 3 (Exocyst complex component Sec6) (Q54BP6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q62825}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q62825}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q62825}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62825}. Midbody {ECO:0000250|UniProtKB:O60645}. Golgi apparatus {ECO:0000250|UniProtKB:O60645}.
Interaction partners:
- Exocyst complex component 6
- Exocyst complex component 1
- Exocyst complex component 2
- Exocyst complex component 7
- Exocyst complex component 5
- Exocyst complex component 8
- Exocyst complex component 4
- Protein transport protein sec1
- Conserved oligomeric Golgi complex subunit 6
- Vacuolar protein sorting-associated protein 54
Sequence:
METVSLVPLEGLDDLSAQSAAIKKIEQNFSNIDSLASVTNHKISLIQQKKTIEAQIKNEVHSELEKSKKGLETLYKSYNRINRMDESFSDTVELCSETSNLIGHYQLIKKVNTVRVNLINILKEVDRLLTIPEKAAEIEQLLSDDLNLLEIHSKLRELERLHQKALKQFESNFEELEAIKEMFSSVPELSHRFENKIWNIVSNSIDIAQIKPAVLVKVAQIIEREKLHEQKQKEKKSQNSLISSEGIHDDDDDDDDTEVNLNNSNKQQNNENENSSSNNNNNYDINNEDEGYDRNRSNYGDRFLEVLIQSISGKFEPMFLNSHNDLVQTLKDVNKMVDELFIVMDIVQECYPPSYDLFNFYVDQYHTKFYSLFGSFSNLMESSHVNNNYQVVVTKNIPSAHILMLVEWVVKNYSRDLSRLGIQDISPPLLDSLDPLIKIYKMHIKQLMREWCDNIINNDNQNKPEVVDGQYCSLAPIQLFESVASQLDIAAATKCQKLVVGVMEEVVSALMYFQVQSITLLQERNHEIKLENVIAYVNNNSKCYDHTQTIVDKVSNILDSEHMGYLDFDPVLEGFLNVSKVATQAISSVIFRDLDECIHKFYTVEWYQEDLMQPIINTFEDYVTNDIQKYILENYLKRLALLLLDTLIEQLLAQLIGGKNKFNENTYKILSNDCDKLLDFFKKYLRLSVVTAKVQILEDFKQMITSSIDMVPVYFRSVINFHKDINERVVELVLYQRTDISKSEITEVLGQIKTIVETVHTDPTNPPTGIFSRMNIYQRGWFS
Protein: Derlin-1 (Degradation in endoplasmic reticulum protein 1) (DERtrin-1) (Der1-like protein 1) (Q9BUN8)
Organism: Homo sapiens (Human)
Function: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. Forms homotetramers which encircle a large channel traversing the endoplasmic reticulum (ER) membrane. This allows the retrotranslocation of misfolded proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome. The channel has a lateral gate within the membrane which provides direct access to membrane proteins with no need to reenter the ER lumen first. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189}; Multi-pass membrane protein {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189}.
Interaction partners:
- Protein sel-1 homolog 1
- Transitional endoplasmic reticulum ATPase
- E3 ubiquitin-protein ligase synoviolin
- E3 ubiquitin-protein ligase AMFR
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Selenoprotein S
- Derlin-2
- Protein OS-9
- Endoplasmic reticulum lectin 1
- Endoplasmic reticulum chaperone BiP
Sequence:
MSDIGDWFRSIPAITRYWFAATVAVPLVGKLGLISPAYLFLWPEAFLYRFQIWRPITATFYFPVGPGTGFLYLVNLYFLYQYSTRLETGAFDGRPADYLFMLLFNWICIVITGLAMDMQLLMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVILGFNYIIGGSVINELIGNLVGHLYFFLMFRYPMDLGGRNFLSTPQFLYRWLPSRRGGVSGFGVPPASMRRAADQNGGGGRHNWGQGFRLGDQ
Protein: Acetyl-CoA acetyltransferase 1 (EC 2.3.1.9) (Acetoacetyl-CoA thiolase 1) (Thiolase 1) (Q9FIK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17120136}. Peroxisome {ECO:0000269|PubMed:17120136}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- 3-hydroxyacyl-CoA dehydrogenase family protein
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
- Acetyl-CoA carboxylase 2
- Acyl-coenzyme A oxidase 4, peroxisomal
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
- Acyl-coenzyme A oxidase 2, peroxisomal
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Acetyl-CoA carboxylase 1
Sequence:
MAPPVSDDSLQPRDVCVVGVARTPIGDFLGSLSSLTATRLGSIAIQAALKRAHVDPALVEEVFFGNVLTANLGQAPARQAALGAGIPYSVICTTINKVCAAGMKSVMLASQSIQLGLNDIVVAGGMESMSNVPKYLPDARRGSRLGHDTVVDGMMKDGLWDVYNDFGMGVCGEICADQYRITREEQDAYAIQSFERGIAAQNTQLFAWEIVPVEVSTGRGRPSVVIDKDEGLGKFDAAKLKKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLHVIAKIRGYADAAQAPELFTTTPALAIPKAIKRAGLDASQVDYYEINEAFSVVALANQKLLGLDPERLNAHGGAVSLGHPLGCSGARILVTLLGVLRAKKGKYGVASICNGGGGASALVLEFMSEKTIGYSAL
Protein: Coiled-coil-helix-coiled-coil-helix domain-containing 10 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial) (Q6PBP6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40
- Transitional endoplasmic reticulum ATPase
- NIMA-related kinase 1.
- Serine/threonine-protein kinase TBK1
- Coiled-coil-helix-coiled-coil-helix domain containing 3a isoform 1
- Sulfhydryl oxidase
- Ataxin-2
Sequence:
MARGSRSRPSPAPASAPAPSYAPAPAAPPPMAVAPAAAQPKQPGLMAQMATTAAGVAVGSAVGHVMGSAITGAFSGGSSSEAPKPAPTYQEPSRLPPSQSGPCLFEVRQFLDCATTQADLSLCEGFNEALKQCKLSSGVTSLV
Protein: SNF2 domain-containing protein CLASSY 1 (Protein CHROMATIN REMODELING 38) (Q9M297)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable chromatin remodeling factor. Required for the initial establishment of DNA methylation and for accumulation of 24-nt siRNAs. May act on RNA templates by remodeling ribonucleoprotein structures and thereby influencing the availability of the RNA to polymerases.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17526749}. Nucleus, nucleolus {ECO:0000269|PubMed:17526749}. Note=In the nucleolus, localized in a ring around the inner periphery.
Interaction partners:
- DNA-directed RNA polymerase IV subunit 1
- RNA-dependent RNA polymerase 2
- Protein SAWADEE HOMEODOMAIN HOMOLOG 1
- Endoribonuclease Dicer homolog 3
- DNA-directed RNA polymerase V subunit 1
- DNA-directed RNA polymerases IV and V subunit 2
- Protein RDM1
- Protein DEFECTIVE IN MERISTEM SILENCING 3
- DNA-directed RNA polymerase V subunit 5A
- Protein RNA-directed DNA methylation 3
Sequence:
MKRKHYFEFNHPFNPCPFEVFCWGTWKAVEYLRIENGTMTMRLLENGQVLDDIKPFQRLRIRSRKATLIDCTSFLRPGIDVCVLYQRDEETPEPVWVDARVLSIERKPHESECLCTFHVSVYIDQGCIGLEKHRMNKVPVLVGLNEIAILQKFCKEQSLDRYYRWRYSEDCSSLVKTRLNLGKFLPDLTWLLVTSVLKNIVFQIRTVHEKMVYQIVTDEDCEGSSSSLSAMNITVEDGVVMSKVVLFNPAEDTCQDSDVKEEIEEEVMELRRSKRRSGRPERYGDSEIQPDSKDGWVRMMPYRYNIWNVSSDDDDEEEDCEDDKDTDDDLYLPLSHLLRKKGSKKGFSKDKQREIVLVDKTERKKRKKTEGFSRSCELSVIPFTPVFEPIPLEQFGLNANSLCGGVSGNLMDEIDKYRSKAAKYGKKKKKKIEMEEMESDLGWNGPIGNVVHKRNGPHSRIRSVSRETGVSEEPQIYKKRTLSAGAYNKLIDSYMSRIDSTIAAKDKATNVVEQWQGLKNPASFSIEAEERLSEEEEDDGETSENEILWREMELCLASSYILDDHEVRVDNEAFHKATCDCEHDYELNEEIGMCCRLCGHVGTEIKHVSAPFARHKKWTTETKQINEDDINTTIVNQDGVESHTFTIPVASSDMPSAEESDNVWSLIPQLKRKLHLHQKKAFEFLWKNLAGSVVPAMMDPSSDKIGGCVVSHTPGAGKTFLIIAFLASYLKIFPGKRPLVLAPKTTLYTWYKEFIKWEIPVPVHLLHGRRTYCMSKEKTIQFEGIPKPSQDVMHVLDCLDKIQKWHAQPSVLVMGYTSFLTLMREDSKFAHRKYMAKVLRESPGLLVLDEGHNPRSTKSRLRKALMKVDTDLRILLSGTLFQNNFCEYFNTLCLARPKFVHEVLVELDKKFQTNQAEQKAPHLLENRARKFFLDIIAKKIDTKVGDERLQGLNMLRNMTSGFIDNYEGSGSGSGDVLPGLQIYTLLMNSTDVQHKSLTKLQNIMSTYHGYPLELELLITLAAIHPWLVKTTTCCAKFFNPQELLEIEKLKHDAKKGSKVMFVLNLVFRVVKREKILIFCHNIAPIRLFLELFENVFRWKRGRELLTLTGDLELFERGRVIDKFEEPGGQSRVLLASITACAEGISLTAASRVIMLDSEWNPSKTKQAIARAFRPGQQKVVYVYQLLSRGTLEEDKYRRTTWKEWVSSMIFSEEFVEDPSQWQAEKIEDDVLREIVEEDKVKSFHMIMKNEKASTGG
Protein: E3 ubiquitin-protein ligase listerin (EC 2.3.2.27) (RING domain mutant killed by rtf1 deletion protein 1) (RING-type E3 ubiquitin transferase listerin) (Q04781)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non-stop proteins) and other translation arrest products induced by poly-lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product. May indirectly play a role in chromatin function and transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:17283062}. Cytoplasm, cytosol {ECO:0000269|PubMed:20835226}.
Interaction partners:
- Ribosome quality control complex subunit 1
- Ribosome quality control complex subunit 2
- Cell division control protein 48
- Nuclear protein localization protein 4
- Ubiquitin fusion degradation protein 1
- E3 ubiquitin-protein ligase HEL2
- General negative regulator of transcription subunit 4
- Protein DOM34
- E3 ubiquitin-protein ligase HUL5
- E3 ubiquitin-protein ligase UBR1
Sequence:
MSFGGINTFQQYNTDLGLGHNGVRISLNYFDGLPDPSLLNSLYSNELKLIFKSLLKRDETTKEKALMDLSNLISDFNQNEYFFNDIFLLCWSQIYAKLIISDYKVIRLQSHQITIMLVKSLRKKISKFLKDFIPLILLGTCELDYSVSKPSLNELTECFNKDPAKINALWAVFQEQLLNLVKEIVVNENEDTISDERYSSKEESEFRYHRVIASAVLLLIKLFVHNKDVSERNSSSLKVILSDESIWKLLNLKNGQNTNAYETVLRLIDVLYTRGYMPSHKNIMKLAVKKLLKSLTHITSKNILKVCPVLPSILNLLATLDDYEDGTIWSYDKSSKEKVLKFLSVSRTSPSPGFFNAVFALYSSTKRHSFLDYYLEWLPFWQKSVQRLNEKGFSARNSAEVLNEFWTNFLKFAEDSSEERVKKMVESEIFNSLSCGKSLSEYTKLNQTLSGVFPPDKWEREIEDYFTSDEDIRKIKVSFEKNLFALLVTSPNNESAISRLFDFFVQLIETDPSNVFNKYDGVYDALNYFLDSDMIFLNGKIGKFINEIPTLVQESTYQNFAGIMAQYSNSKFFKMNTDAITSLEDFFIVALSFNLPKTIILATMNELDNDIYQQLMKSDSLELELYIEDFMKNYKFDDSGEIFKGNNKFLNQRTITTLYRSAVANGQVEQFCAVLSKLDETFFSTLLLNTDFLSCALYEVSEDTNEKLFKLSLQLAKGNSEIANKLAQVILQHAQVYFSPGAKEKYVTHAVELINGCNDTSQIFFPANAIEVFARYMPAIDYRSSLVSSLSTNTHLLLTDDKPINLKNMQKLIRYALFLDALLDALPERVNNHIVAFITVVSELVTDYNCLSEEPNDLYYDFGHTFFKHGKVNLNFSDIVGNVIQPANGGDAMLTFDIAESNSVYFFYYSRVLYKVLLNSIDTVSSTTLNGLLASVESFVTKTVRDQKSTDKDYLLCAILLLMFNRSNSKDEITKLRTLLASQLIGIREVELVDQEFKSLALLNNLLDIPQADKQFVPIAPQRLNMIFRSILKWLDSDLAYEPSFSTVRLLLLDFFTKLMRFEGVRDMGITAFELSERLLADSLSMCQIDDTLYLLELRSSCLNLYETLSQGVSKNGEEISEYGDEIQENLIELMFLNFNQERNNQVSTLFYQKLYKVISSMELKKLESQYKRIFEVVLNDKDIGSNINQSRLLTTLLGSLVVKTQQDIIIEYELRIQKQTGSDVDGSASDNDVNSKFKLPQKLLQKVTDEVPKEYLEYENKNSFIKYLWYWHLILMYFKDTSYNMRQIFIEQLKEAGLINRMFDFITDQIDLRDTEFWKQVDTKEISEYNIVGNNFSPYKEDIFEECKKLLGHTLYQLFNNVGCLTSIWWLNIKDRTLQNDIEKFVSEFISPILIKNEFDDINSKMDRLTSNDDALTIKLNNITNEVKASYLIDDQKLEISFKLPKNYPLTNIQVNGVSRVGISEQKWKQWIMSTQHVITGMNGSVLDSLELFTKNVHLQFSGFEECAICYSILHAVDRKLPSKTCPTCKNKFHGACLYKWFRSSGNNTCPLCRSEIPFRR
Protein: Calcium-activated chloride channel regulator 1 (EC 3.4.-.-) (Calcium-activated chloride channel family member 1) (hCLCA1) (Calcium-activated chloride channel protein 1) (CaCC-1) (hCaCC-1) (A8K7I4)
Organism: Homo sapiens (Human)
Function: May be involved in mediating calcium-activated chloride conductance. May play critical roles in goblet cell metaplasia, mucus hypersecretion, cystic fibrosis and AHR. May be involved in the regulation of mucus production and/or secretion by goblet cells. Involved in the regulation of tissue inflammation in the innate immune response. May play a role as a tumor suppressor. Induces MUC5AC.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:15919655}. Cell membrane {ECO:0000269|PubMed:15919655}; Peripheral membrane protein {ECO:0000269|PubMed:15919655}; Extracellular side {ECO:0000269|PubMed:15919655}. Note=Protein that remains attached to the plasma membrane appeared to be predominantly localized to microvilli.
Interaction partners:
- Anoctamin-2
- Zymogen granule membrane protein 16
- Calcium-activated chloride channel regulator 4
- Calcium-activated chloride channel regulator 2
- Plasminogen activator inhibitor 2
- Periostin
- Anoctamin-1
- IgGFc-binding protein
- Cystic fibrosis transmembrane conductance regulator
- Calcineurin B homologous protein 2
Sequence:
MGPFKSSVFILILHLLEGALSNSLIQLNNNGYEGIVVAIDPNVPEDETLIQQIKDMVTQASLYLLEATGKRFYFKNVAILIPETWKTKADYVRPKLETYKNADVLVAESTPPGNDEPYTEQMGNCGEKGERIHLTPDFIAGKKLAEYGPQGRAFVHEWAHLRWGVFDEYNNDEKFYLSNGRIQAVRCSAGITGTNVVKKCQGGSCYTKRCTFNKVTGLYEKGCEFVLQSRQTEKASIMFAQHVDSIVEFCTEQNHNKEAPNKQNQKCNLRSTWEVIRDSEDFKKTTPMTTQPPNPTFSLLQIGQRIVCLVLDKSGSMATGNRLNRLNQAGQLFLLQTVELGSWVGMVTFDSAAHVQNELIQINSGSDRDTLAKRLPAAASGGTSICSGLRSAFTVIRKKYPTDGSEIVLLTDGEDNTISGCFNEVKQSGAIIHTVALGPSAAQELEELSKMTGGLQTYASDQVQNNGLIDAFGALSSGNGAVSQRSIQLESKGLTLQNSQWMNGTVIVDSTVGKDTLFLITWTMQPPQILLWDPSGQKQGGFVVDKNTKMAYLQIPGIAKVGTWKYSLQASSQTLTLTVTSRASNATLPPITVTSKTNKDTSKFPSPLVVYANIRQGASPILRASVTALIESVNGKTVTLELLDNGAGADATKDDGVYSRYFTTYDTNGRYSVKVRALGGVNAARRRVIPQQSGALYIPGWIENDEIQWNPPRPEINKDDVQHKQVCFSRTSSGGSFVASDVPNAPIPDLFPPGQITDLKAEIHGGSLINLTWTAPGDDYDHGTAHKYIIRISTSILDLRDKFNESLQVNTTALIPKEANSEEVFLFKPENITFENGTDLFIAIQAVDKVDLKSEISNIARVSLFIPPQTPPETPSPDETSAPCPNIHINSTIPGIHILKIMWKWIGELQLSIA
Protein: cAMP-dependent protein kinase catalytic subunit PRKX (PrKX) (Protein kinase X) (Protein kinase X-linked) (Serine/threonine-protein kinase PRKX) (EC 2.7.11.1) (PKA-related protein kinase) (Q922R0)
Organism: Mus musculus (Mouse)
Function: Serine/threonine protein kinase regulated by and mediating cAMP signaling in cells. Acts through phosphorylation of downstream targets that may include CREB, SMAD6 and PKD1 and has multiple functions in cellular differentiation and epithelial morphogenesis. Regulates myeloid cell differentiation through SMAD6 phosphorylation. Involved in nephrogenesis by stimulating renal epithelial cell migration and tubulogenesis. Also involved in angiogenesis through stimulation of endothelial cell proliferation, migration and vascular-like structure formation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=cAMP induces nuclear translocation. {ECO:0000250}.
Interaction partners:
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- cAMP-dependent protein kinase type I-beta regulatory subunit
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- cAMP-dependent protein kinase type II-beta regulatory subunit
- Lysine-specific demethylase 5D
- Histone demethylase UTY demethylase UTY)
Sequence:
MEPPAGAAATVKDPDHDPVKTKVSAPAADPKPRTSSQKAGHSLQDWDTIATVGTGTFGRVNLVKEKTGRQYCALKIMSIPDVIRLKQEQHVQNEKAVLKEINHPFLIKLLWTGHDNRFLYMLMEFVPGGELFTYLRNRGRFSSVASVFYATEIVCAIEYLHSKEIVYRDLKPENILLDREGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSGFPPFFDDNPFGIYQKILACKIDFPRQLDFTSKDLIKKLLVVDRTRRLGNMKNGAEDIKRHRWFRGVEWESVPQRKLKPPIVPKLSGDGDISNFETYPESELDKTPSVSDKDLETFKNF
Protein: Sodium/potassium-transporting ATPase subunit alpha-1 (Na(+)/K(+) ATPase alpha-1 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-1) (P06685)
Organism: Rattus norvegicus (Rat)
Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8VDN2}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:16914892}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:29499166}. Melanosome {ECO:0000250|UniProtKB:P05023}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-3
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit beta-2
- Protein ATP1B4
- Phospholemman
- Sodium/potassium-transporting ATPase subunit alpha-2
- cAMP-dependent protein kinase catalytic subunit alpha
- Sodium/potassium-transporting ATPase subunit alpha-3
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MGKGVGRDKYEPAAVSEHGDKKSKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSATEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWFALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIEVCCGSVMEMREKYTKIVEIPFNSTNKYQLSIHKNPNASEPKHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDEVNFPVDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDAKACVVHGSDLKDMTSEELDDILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIVGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRETWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGAALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY