wanglab/gogpt-training-data huggingface dataset:
Protein: Taste receptor type 2 member 14 (T2R14) (Taste receptor family B member 1) (TRB1) (Q9NYV8)
Organism: Homo sapiens (Human)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein {ECO:0000269|PubMed:38600377, ECO:0000269|PubMed:38776963}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Taste receptor type 1 member 2
- Taste receptor type 1 member 3
Sequence:
MGGVIKSIFTFVLIVEFIIGNLGNSFIALVNCIDWVKGRKISSVDRILTALAISRISLVWLIFGSWCVSVFFPALFATEKMFRMLTNIWTVINHFSVWLATGLGTFYFLKIANFSNSIFLYLKWRVKKVVLVLLLVTSVFLFLNIALINIHINASINGYRRNKTCSSDSSNFTRFSSLIVLTSTVFIFIPFTLSLAMFLLLIFSMWKHRKKMQHTVKISGDASTKAHRGVKSVITFFLLYAIFSLSFFISVWTSERLEENLIILSQVMGMAYPSCHSCVLILGNKKLRQASLSVLLWLRYMFKDGEPSGHKEFRESS
Protein: Protein-arginine deiminase type-3 (EC 3.5.3.15) (Peptidylarginine deiminase III) (Protein-arginine deiminase type III) (Q9ULW8)
Organism: Homo sapiens (Human)
Function: Catalyzes the deimination of arginine residues of proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27866708}.
Interaction partners:
- Trichohyalin
- Filaggrin-2
- Filaggrin
- Protein S100-A3
Sequence:
MSLQRIVRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGRERADTRRWRFDATLEIIVVMNSPSNDLNDSHVQISYHSSHEPLPLAYAVLYLTCVDISLDCDLNCEGRQDRNFVDKRQWVWGPSGYGGILLVNCDRDDPSCDVQDNCDQHVHCLQDLEDMSVMVLRTQGPAALFDDHKLVLHTSSYDAKRAQVFHICGPEDVCEAYRHVLGQDKVSYEVPRLHGDEERFFVEGLSFPDAGFTGLISFHVTLLDDSNEDFSASPIFTDTVVFRVAPWIMTPSTLPPLEVYVCRVRNNTCFVDAVAELARKAGCKLTICPQAENRNDRWIQDEMELGYVQAPHKTLPVVFDSPRNGELQDFPYKRILGPDFGYVTREPRDRSVSGLDSFGNLEVSPPVVANGKEYPLGRILIGGNLPGSSGRRVTQVVRDFLHAQKVQPPVELFVDWLAVGHVDEFLSFVPAPDGKGFRMLLASPGACFKLFQEKQKCGHGRALLFQGVVDDEQVKTISINQVLSNKDLINYNKFVQSCIDWNREVLKRELGLAECDIIDIPQLFKTERKKATAFFPDLVNMLVLGKHLGIPKPFGPIINGCCCLEEKVRSLLEPLGLHCTFIDDFTPYHMLHGEVHCGTNVCRKPFSFKWWNMVP
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Q1WEZ6)
Organism: Sus scrofa (Pig)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000369}.
Interaction partners:
Sequence:
MFVNRWLYSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWAVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNQAWAKIHFVIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTAWNTISSMGSFISLTAVMLMIFIIWEAFASKREVSAVELTSTNLEWLHGCPPPYHTFEEPTYINLK
Protein: Coiled-coil-helix-coiled-coil-helix domain containing 2, isoform A (RE73921p) (Q9VX77)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MIP04261p
- Vacuolar protein sorting-associated protein 35
- Coiled-coil-helix-coiled-coil-helix domain containing 3
- Cytochrome c-2
- Serine/threonine-protein kinase Pink1, mitochondrial
- Cytochrome c-1
Sequence:
MVRRGRSASPPPSTRRTAPVQARAPAPAPAPVQTRAPAPAASAPVPAPMSAPPSAVGMPAPQQPSMFQQMAATAGGVAVGSAIGHTVGHGLTSLFSGSGDKEAAAPAPAAAAPAPQQPYYAQQQQPNEPQGACAWELKQFIQCAQGQADLTLCEGFNEALRQCKQSHHLQ
Protein: DNA-directed RNA polymerases II subunit, putative (EC 2.7.7.6) (Q388R5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA-dependent RNA polymerases, putative
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase subunit beta
Sequence:
MSSESYAIGQEELVYDRMFRVMRTVGEMMRDRKYQVPSSIIPETVGQFCEQYVDREGRRIYRERMTVPCERVGGTHRSRAMVFFASELGMEGMKGYCQTAMDANCERVIIVTHGKVNATVKRYVDCINRSGTGQKVQLFDEDDLVVNITHHELVPKHTQLEDEEVKEMLEAHSLELNMLPRILSTDPVAAYLGLERGRVVRIERKSVSAGFYVTYRQVV
Protein: Ceramide synthase 2 (E7F9X7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- 3-dehydrosphinganine reductase
- Sphingosine kinase 2.
- Sphingosine kinase 1.
- Delta
- sphingolipid 4-desaturase
- UDP-glucose ceramide glucosyltransferase.
- Sphingosine-1-phosphate phosphatase 1.
- Sphingosine-1-phosphate phosphatase 2
- Si:ch211-212g7.6
- Ceramide kinase family protein
Sequence:
MLAGLSELFWQERLWFPEGLGWADLEDRDGRVYAKARDLWVALPIAVLFLLIRQLFEKYVATPLASLLGLKETVRRRVAHNPALESYYCNTSKNPTQSSVEKLSKQTGWTERQVQRWFRRRRNQDRPNLLKKFCEASWRFAFYLLAFIGGLAALIDKPWLYDLEEMWKGFPTLTLLPSQYWYYMLELAFYTSLLFSVASDVKRKDFKEQIIHHVATILLISFSWCVNYIRAGTLIMFMHDSADYLLESAKMFNYARWKNACNYIFILFAAIFIVTRLIIFPFRIMYCTWVYPVTLYPPFFGYYFFNGLLMVLLCLHMFWAALIIRLAFRFLSSNSSVEDERSDRDETDESEEEEELKNGEIKKKNGAAQNGHATYNNNHSKTE
Protein: Crooked neck-like protein 1 (Crooked neck homolog) (Crooked neck protein) (P63155)
Organism: Rattus norvegicus (Rat)
Function: Involved in pre-mRNA splicing process.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BZJ0}. Nucleus speckle {ECO:0000250|UniProtKB:Q9BZJ0}. Note=Colocalizes with core spliceosomal snRNP proteins. {ECO:0000250|UniProtKB:Q9BZJ0}.
Interaction partners:
- Pre-mRNA-splicing factor SYF1
- Pre-mRNA-splicing factor ISY1 homolog
- SNW domain-containing protein 1
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor RBM22
- Protein BUD31 homolog
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-processing factor 19
- RNA helicase aquarius
- Cell division cycle 5-like protein
Sequence:
MAASTAAGKQRIPKVAKVKNKAPAEVQITAEQLLREAKERELELLPPPPQQKITDEEELNDYKLRKRKTFEDNIRKNRTVISNWIKYAQWEESLKEIQRARSIYERALDVDYRNITLWLKYAEMEMKNRQVNHARNIWDRAITTLPRVNQFWYKYTYMEEMLGNVAGARQVFERWMEWQPEEQAWHSYINFELRYKEVERARTIYERFVLVHPAVKNWIKYARFEEKHAYFAHARKVYERAVEFFGDEHMDEHLYVAFAKFEENQKEFERVRVIYKYALDRISKQEAQELFKNYTIFEKKFGDRRGIEDIIVSKRRFQYEEEVKANPHNYDAWFDYLRLVESDAEADTVREVYERAIANVPPIQEKRHWKRYIYLWVNYALYEELEAKDPERTRQVYQASLELIPHKKFTFAKMWLYYAQFEIRQKNLPFARRALGTSIGKCPKNKLFKGYIELELQLREFDRCRKLYEKFLEFGPENCTSWIKFAELETILGDIERARAIYELAISQPRLDMPEVLWKSYIDFEIEQEETERTRNLYRQLLQRTQHVKVWISFAQFELSSGKEGSVAKCRQIYEEANKTMRNCEEKEERLMLLESWRSFEDEFGTVSDKERVDKLMPEKVKKRRKVQADDGSDAGWEEYYDYIFPEDAANQPNLKLLAMAKLWKKQQQEREAAEQDPDKDIDESESSSF
Protein: Ankyrin repeat and SAM domain-containing protein 6 (Polycystic kidney disease protein 1) (SamCystin) (Sterile alpha motif domain-containing protein 6) (SAM domain-containing protein 6) (P0C0T2)
Organism: Rattus norvegicus (Rat)
Function: Required for renal function.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q6GQX6}. Cytoplasm {ECO:0000269|PubMed:19324013}. Note=Localizes to the proximal region of the primary cilium in the presence of INVS. {ECO:0000250|UniProtKB:Q6GQX6}.
Interaction partners:
- Serine/threonine-protein kinase Nek8
- Nephrocystin-3
- Ankyrin repeat and SAM domain-containing protein 3
- Serine/threonine-protein kinase Nek7
- Inversin
- Nephrocystin-1
Sequence:
MGEGALAPGLQLLLRACEQGDTDTARRLLEPGGEPVAGSEAGAEPAGPEAARAVEAGTPVPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGESTASGGSRDELLGITALMAAVQHGHEAVVRLLMEWGADPNHTARTVGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYLDPLTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIADEDPNHVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADMNKQDSVHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVRLLASVCMQVNKDRGGRPSHRPPLPHSKARQPWSIPMLPDDKGGLKSWWSRMSNRFRKLKLMQTLPRGLAANQPLPFSDEPELALDSTMRAPPQDRTNHLGPPEAAHAAKDSGPGNPRREKDDVLLTTMLRNGAPFPRLPSDKLKAVIPPFLPPSSFELWSSDRSRTCPNGKADPMKTVLPPRASRAHPVGCVGTDGAAGRPVKFPSISRSPTSPASSGNFNHSPHSSGGASGVGSMSRLGGELHNRSGGSVDSVLSQIAAQRKKAAGLCEQKPPCQQSSPVGPATGSSPPELPASLLGSGSGSSNVTSSSKKLDPGKRPPSGTSATSKSTSPTLTPSPSPKGHTAESSVSSSSSHRQSKSSGGSSSGTITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNAGKGRERQILQETIHNFHSSFESSASNTRAPGNSPCMAGWVRPEETVSSRR
Protein: R-spondin 2 (R-spondin-2 precursor) (F1Q5C9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- E3 ubiquitin-protein ligase znrf3
- Leucine-rich repeat-containing G-protein coupled receptor 4
- R-spondin-3
- R-spondin-1
Sequence:
MQFRLFSFALIVLNCVDYSHCQTQQSHRWRRNKRASYGAYPICKGCSVCSKDNGCMNCQPKLFLFLRRERMRQYGECLHACPSGYYGMRGTEINMCSRCRIDDCEACFSKDFCTKCKLGFYLHKGRCFEKCPEGFAPLEDTMECGEGCEVGQWSEWGTCARRNKTCGFKWGLETRTRHIVKKPPKDTIPCPTIAESRRCKMAMRHCRKGGSGKGHRTKDQKKKSNKQRLRLRAQNQHSDHLASIRAGQ
Protein: RNA polymerase sigma factor (O32728)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Interaction partners:
Sequence:
MDVDVKQGQSPIKDQEMKELIRRSQEGDQEARDEIIEKNMRLVWSVVQRFLNRGYEADDLFQIGCIGLLKSVDKFDLSYDVKFSTYAVPMIIGEIQRFLRDDGTVKVSRSLKEMGNKIRKAKDELSKTRGRSPTITEIADHLGISPEDVVLAQEAVRLPTSIHETVYENDGDPITLLDQIADADEASWFDKIALKKAIEELDERERLIVYLRYYRDRTQSEVASRLGISQVQVSRLEKKILQHIKDKMDG
Protein: Elongator complex protein 4 (G5E9D4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAVATCGSVAASTGSAVATASKSNVTSFQRRGPRASVTNDSGPRLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELPAPLLDDKCKKEFDEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPEKISSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIEAGVQWHDLGSRQPRLLGSSNSPASASLVAGITGAHHHTQLIFVFLVEMGFHHVGQAGLELLTSGDSSASASQSAGITGMSYRARPRALYFKENKSKVGARQLLETREEHLSSRLLILTQAERLCMGRRFFTAFHIFNELPCKGDCICLQTCQTQ
Protein: Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (F4J6A1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03006}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit K
Sequence:
MTIDSQQKTSKFRWGEMDEDEDLDFLLPPKQVIGPDENGLKTTIEYKFNDEENKVKITTRTRVRKLASARLNKRAMERRNWPKFGDAANEEAGSHLTMVSTEEILLERPRAPGDQLANHMLASIPEYELKCALTFVAANCTKADESKATGDGLSQLGKGGAVLMVCRICHKKGDHWTSKCPYKDLAAPTDVFIDKPPTGESSTMSAAPGTGKAAYVPPSMRAGADRSAVGSDMRRRNDENSVRVTNLSEDTREPDLMELFHPFGAVTRVYVAIDQKTGVSRGFGFVNFVSREDAQRAINKLNGYGYDNLILRVEWATPRPT
Protein: Aminoaldehyde dehydrogenase 2 (SlAMADH2) (EC 1.2.1.-) (4-trimethylammoniobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.47) (Aminobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.19) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.54) (B6ECN9)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively.
Interaction partners:
Sequence:
MAIPNIRIPCRQLFIDGEWREPLKKNRLPIINPANEEIIGYIPAATEEDVDMAVKAARSALRRDDWGSTTGAQRAKYLRAIAAKVLEKKPELATLETIDNGKPWFEAASDIDDVVACFEYYADLAEALDSKKQTEVKLHLDSFKTHVLREPLGVVGLITPWNYPLLMTTWKVAPALAAGCAAILKPSELASITSLELGEICREVGLPPGALSILTGLGHEAGSPLVSHPDVDKIAFTGSGPTGVKIMTAAAQLVKPVTLELGGKSPIVVFDDIHNLDTAVEWTLFGCFWTNGQICSATSRLIIQETIAPQFLARLLEWTKNIKISDPLEEDCKLGPVISRGQYEKILKFISTAKDEGATILYGGDRPEHLKKGYYIQPTIITDVDTSMEIWKEEVFGPVLCVKTFKIEEEAIELANDTKFGLGAAILSKDLERCERFTKAFQSGIVWINCSQPCFWQPPWGGKKRSGFGRELGEWSLENYLNIKQVTQYVTPDEPWAFYKSPSKL
Protein: Arrestin domain-containing protein 2 (Q8TBH0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLFDKVKAFSVQLDGATAGVEPVFSGGQAVAGRVLLELSSAARVGALRLRARGRAHVHWTESRSAGSSTAYTQSYSERVEVVSHRATLLAPDTGETTTLPPGRHEFLFSFQLPPTLVTSFEGKHGSVRYCIKATLHRPWVPARRARKVFTVIEPVDINTPALLAPQAGAREKVARSWYCNRGLVSLSAKIDRKGYTPGEVIPVFAEIDNGSTRPVLPRAAVVQTQTFMARGARKQKRAVVASLAGEPVGPGQRALWQGRALRIPPVGPSILHCRVLHVDYALKVCVDIPGTSKLLLELPLVIGTIPLHPFGSRSSSVGSHASFLLDWRLGALPERPEAPPEYSEVVADTEEAALGQSPFPLPQDPDMSLEGPFFAYIQEFRYRPPPLYSEEDPNPLLGDMRPRCMTC
Protein: Ribonuclease inhibitor (Placental ribonuclease inhibitor) (Placental RNase inhibitor) (Ribonuclease/angiogenin inhibitor 1) (RAI) (P13489)
Organism: Homo sapiens (Human)
Function: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23843625, ECO:0000305|PubMed:3219362}. Nucleus {ECO:0000269|PubMed:23843625}. Note=Localizes in the cytoplasm in absence of stress; translocates to the nucleus in response to stress. {ECO:0000269|PubMed:23843625}.
Interaction partners:
- Angiogenin
- Ribonuclease pancreatic
- Non-secretory ribonuclease
- Microprocessor complex subunit DGCR8
- F-box only protein 38
- F-box only protein 39
- F-box only protein 33
- Ribonuclease 3
- Exportin-5
- Endoribonuclease Dicer
Sequence:
MSLDIQSLDIQCEELSDARWAELLPLLQQCQVVRLDDCGLTEARCKDISSALRVNPALAELNLRSNELGDVGVHCVLQGLQTPSCKIQKLSLQNCCLTGAGCGVLSSTLRTLPTLQELHLSDNLLGDAGLQLLCEGLLDPQCRLEKLQLEYCSLSAASCEPLASVLRAKPDFKELTVSNNDINEAGVRVLCQGLKDSPCQLEALKLESCGVTSDNCRDLCGIVASKASLRELALGSNKLGDVGMAELCPGLLHPSSRLRTLWIWECGITAKGCGDLCRVLRAKESLKELSLAGNELGDEGARLLCETLLEPGCQLESLWVKSCSFTAACCSHFSSVLAQNRFLLELQISNNRLEDAGVRELCQGLGQPGSVLRVLWLADCDVSDSSCSSLAATLLANHSLRELDLSNNCLGDAGILQLVESVRQPGCLLEQLVLYDIYWSEEMEDRLQALEKDKPSLRVIS
Protein: Voltage-dependent calcium channel gamma-7 subunit (Neuronal voltage-gated calcium channel gamma-7 subunit) (Transmembrane AMPAR regulatory protein gamma-7) (TARP gamma-7) (P62955)
Organism: Homo sapiens (Human)
Function: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit. Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Displays subunit-specific AMPA receptor regulation. Shows specificity only for GRIA1 and GRIA2.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21127204}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent calcium channel gamma-4 subunit
- Voltage-dependent calcium channel gamma-8 subunit
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent calcium channel gamma-3 subunit
- Voltage-dependent L-type calcium channel subunit beta-4
- Voltage-dependent calcium channel gamma-6 subunit
- Voltage-dependent calcium channel subunit alpha-2/delta-4
Sequence:
MSHCSSRALTLLSSVFGACGLLLVGIAVSTDYWLYMEEGTVLPQNQTTEVKMALHAGLWRVCFFAGREKGRCVASEYFLEPEINLVTENTENILKTVRTATPFPMVSLFLVFTAFVISNIGHIRPQRTILAFVSGIFFILSGLSLVVGLVLYISSINDEVMNRPSSSEQYFHYRYGWSFAFAASSFLLKEGAGVMSVYLFTKRYAEEEMYRPHPAFYRPRLSDCSDYSGQFLQPEAWRRGRSPSDISSDVSIQMTQNYPPAIKYPDHLHISTSPC
Protein: Ribosomal protein L7Ae/L30e/S12e/Gadd45 family protein (F4K455)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus, nucleolus {ECO:0000256|RuleBase:RU366039}.
Interaction partners:
- Protein SLOW WALKER 1
- U3 snoRNP-associated protein-like YAO
- U3 snoRNP-associated protein-like EMB2271
- Nucleolar protein 56
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex subunit 3-like protein
- U3 small nucleolar RNA-associated protein 18 homolog
- Uncharacterized protein At3g06530
- M phase phosphoprotein 10
- Probable nucleolar protein 5-1
Sequence:
MTGEVVNPKAYPLADSQLSITILDLVQQATNYKQLKKGANEGIRLLLMCVCLSYLLSLMFVKLFLIYLNLFISATKTLNRGISEFVVMAADAEPLEILLHLPLLAEDKNVPYVFVPSKQALGRACGVTRPVIACSVTSNEASQLKSQIQHLKDAIEKLLI
Protein: U6 snRNA-associated Sm-like protein LSm3 (Q8IGW7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365046}.
Interaction partners:
Sequence:
MADETEQLSQVILPVKEPLDLIRLSLDEKVYVKMRNERELRGRLHAFDQHLNMVLGDAEETVTTVEIDEETYEEVYKTAKRTIPMLFVRGDGVILVSPPMRVD
Protein: Protein RecA (Recombinase A) (P62217)
Organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
Sequence:
MGESIMKKAKEDAPSVDDSKKLAIEQAMSQIEKQFGKGSIMKLGSDSAKQTVQVIPSGSLDLDIALGIGGYPIGRIVEIYGPESSGKTTLTLSAIAEAQKRGGVAAFIDAEHALDPSYAKKLGVNIDELLVSQPDNGEEALEICESLVRSNAIDLIVIDSVAALVPKAEIEGDMGDSHMGLQARLMSQALRKLTGTIAKSKTVVIFINQIRMKIGVMFGSPETTTGGNALKFYCSVRLDIRKIETIKEKEESVGNRVRVKVVKNKCAPPFKQAEFDIIFNAGISREGSLVDLGVKHDIIHKAGAWYSYNTEKIGQGKEAAKEYLKNNPEIALTIENMVRDLNSLPLLVQENNKKSRKEEKLEQAAG
Protein: Inhibitory regulator protein BUD2/CLA2 (Bud site selection protein 2) (P33314)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Stimulates the GTPase activity of BUD1/RSR1. Participates in the regulation of bud-site selection.
Interaction partners:
- Ras-related protein RSR1
- Bud site selection protein 5
- Bud emergence protein 1
- Bud site selection protein 4
- Bud site selection protein 3
- Cell division control protein 24
- G1/S-specific cyclin CLN2
- Cell division control protein 42
- Axial budding pattern protein 2
- Bud site selection protein 9
Sequence:
MSSNNEPAQSRTSYFKLNEFLSNVKHYKNTFKGEIQWCNNLSLNDWKTHYLQITSTGALTHSIDELTADSTNIQPIIKHLQQCRIEIIKDKHSSFKDINANCNFIIQVNTSGKDNKVYLRVKSWSDFKKLLTCLIWWSSMKTNGIFNKFQVSRPLEFKSKKMAKPESLLVYKLNVFGPIVKNIVLPPATNILESPDIINNDDNSVGWFSAMGVLKSNGMLDLLLQSDGSLIYSLNISQLLRSEIRILDSSVLQSENSLFLGELPLLRSQLGLEKFRIENIASAATNSSDISQEIIVEFPLRIDLEDCFIALQSFARSEYLSITGSDKSNDMKISNSFKISILEANFQSINLNDKNNTPWSIFTDITAWGHTWARTSMVSNSSNPFWREEFQFNELLRLTNSYLEIKQLFHDLNNKKRLRLIGKIKITQEIINDTRYNKETRLPIMDVDNKNFQIGTICIKISSNLNFILPSTNFVKLEKLLMNANLSMVSNLIYKSSSSMENDNKLTQTSIIFLDIFQSLSRIEEWFHVLIDKELAKIDGTVSRINQKNLDSKHVFNSLFRGNSILTKSIEQYFFRVGNEYLSKALSAILKEIIESNKSCELDPARVKEKDEVKKRKIIADNYKRLYSWVTKIWKRLYATSNDLPIEIRNVLKIFRQKLEIICIDDTLQIILNGISGLLFLRFFCPVILNPKLFKYVSQNLNETARRNLTLISKVLLNLSTLTQFANKEPWLMKMNNFIDKRHNDLLDYIDKMTQKKLDFNSKILNLSSTISRPKLAIEQTMLDDLPQIPYLLDKNLRETEFVNLIVNFSQEDMTKMEKYNHMDNGGKGELIEEEGLLSGSSLNLSVDKKDLDSPIEVKPEIGELEFEKITENNTEIFGDDLMNLLKSDDVGSRSRDLDNGANSGIKFNSIIPKAEEEKHAMKELEQESCLLYNRINHIRKRLSGYECASSTLFEDKKYSISLSHKIFYEEIKEGKEIVLKLLNKPTNENSSARLQKFFTKGVSSKSNNTVGDSYCKFLTIDVSDENPKSSNKTSVHGTSSENGAKDDYLTLPNSQGKGNLGNRFSPTKLSRIMRKPPNADVPKEQNSRKLTRWFKKKKETGGS
Protein: Myelin basic protein (E7EYA2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Myelin membrane {ECO:0000256|ARBA:ARBA00004392}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004392}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004392}.
Interaction partners:
- DMalpha2b
- DMalpha1
- STIM-activating enhance
- Myelin basic protein
- Band 4.1-like protein 3a isoform 1
Sequence:
MGQHLGKREPLSVSKGSSTVSEHINSTDTPAESQDEVFGLGEADLNQNNGCSSKSPVVTDSMNAEVHHSSWNQPNTVDPNASGPRPHLVRLFSRDAPGREDNTFKDRPSESDELQTIHEHGGAGSECESEGTE
Protein: Interleukin-17A (IL-17) (IL-17A) (Cytotoxic T-lymphocyte-associated antigen 8) (CTLA-8) (Q61453)
Organism: Rattus norvegicus (Rat)
Function: Effector cytokine of innate and adaptive immune system involved in antimicrobial host defense and maintenance of tissue integrity. Signals via IL17RA-IL17RC heterodimeric receptor complex, triggering homotypic interaction of IL17RA and IL17RC chains with TRAF3IP2 adapter. This leads to downstream TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways ultimately resulting in transcriptional activation of cytokines, chemokines, antimicrobial peptides and matrix metalloproteinases, with potential strong immune inflammation. Plays an important role in connecting T cell-mediated adaptive immunity and acute inflammatory response to destroy extracellular bacteria and fungi. As a signature effector cytokine of T-helper 17 cells (Th17), primarily induces neutrophil activation and recruitment at infection and inflammatory sites. In airway epithelium, mediates neutrophil chemotaxis via induction of CXCL1 and CXCL5 chemokines. In secondary lymphoid organs, contributes to germinal center formation by regulating the chemotactic response of B cells to CXCL12 and CXCL13, enhancing retention of B cells within the germinal centers, B cell somatic hypermutation rate and selection toward plasma cells. Effector cytokine of a subset of gamma-delta T cells that functions as part of an inflammatory circuit downstream IL1B, TLR2 and IL23A-IL12B to promote neutrophil recruitment for efficient bacterial clearance. Effector cytokine of innate immune cells including invariant natural killer cell (iNKT) and group 3 innate lymphoid cells that mediate initial neutrophilic inflammation. Involved in the maintenance of the integrity of epithelial barriers during homeostasis and pathogen infection. Upon acute injury, has a direct role in epithelial barrier formation by regulating OCLN localization and tight junction biogenesis. As part of the mucosal immune response induced by commensal bacteria, enhances host's ability to resist pathogenic bacterial and fungal infections by promoting neutrophil recruitment and antimicrobial peptides release. In synergy with IL17F, mediates the production of antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry of microbes through the epithelial barriers. Involved in antiviral host defense through various mechanisms.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q62386}.
Interaction partners:
- Interleukin-17 receptor A
- Interleukin-17 receptor C
- T-cell surface glycoprotein CD4
- Tumor necrosis factor
- Interferon gamma
- Interleukin-17F
- Interleukin 22
- Interleukin-6
- Interleukin-10
- Interleukin-2
Sequence:
MCLMLLLLLNLEATVKAAVLIPQSSVCPNAEANNFLQNVKVNLKVINSLSSKASSRRPSDYLNRSTSPWTLSRNEDPDRYPSVIWEAQCRHQRCVNAEGKLDHHMNSVLIQQEILVLKREPEKCPFTFRVEKMLVGVGCTCVSSIVRHAS