wanglab/gogpt-training-data huggingface dataset:
Protein: Procollagen galactosyltransferase 1 (EC 2.4.1.50) (Collagen beta(1-O)galactosyltransferase 1) (ColGalT 1) (Glycosyltransferase 25 family member 1) (Hydroxylysine galactosyltransferase 1) (Q8NBJ5)
Organism: Homo sapiens (Human)
Function: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. By acting on collagen glycosylation, facilitates the formation of collagen triple helix. Also involved in the biosynthesis of collagen type IV.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:20470363}. Note=Colocalized with PLOD3 and mannose binding lectin/MBL2. {ECO:0000269|PubMed:20470363}.
Interaction partners:
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- Procollagen galactosyltransferase 2
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-2
- Collagen alpha-2
Sequence:
MAAAPRAGRRRGQPLLALLLLLLAPLPPGAPPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVAVKSLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTVVAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDIIVFAFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHPPAEPSRFISAPTKTPDKMGFDEVFMINLRRRQDRRERMLRALQAQEIECRLVEAVDGKAMNTSQVEALGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRGLQKSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPRVRNLVEADYSYWTLAYVISLQGARKLLAAEPLSKMLPVDEFLPVMFDKHPVSEYKAHFSLRNLHAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEHVKTDWDRAKSQKMREQQALSREAKNSDVLQSPLDSAARDEL
Protein: Pachytene checkpoint protein 2 homolog (AtPCH2) (Q8H1F9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a key role in chromosome recombination during meiosis. Mediates meiotic chromosome remodeling and crossover maturation.
Subcellular location: Chromosome {ECO:0000269|PubMed:26182244}. Note=Localizes to the sites of chromosome axis remodeling. {ECO:0000269|PubMed:26182244}.
Interaction partners:
- Mitotic spindle checkpoint protein MAD2
- DNA polymerase zeta processivity subunit
- Meiotic recombination protein DMC1 homolog
- Protein DOUBLE-STRAND BREAK FORMATION
- Cytochrome c1 2, heme protein, mitochondrial
- Cytochrome c1 1, heme protein, mitochondrial
- DNA replication licensing factor MCM7
- Kinetochore protein NUF2 homolog
- Protein PUTATIVE RECOMBINATION INITIATION DEFECT 1
- Exonuclease 1
Sequence:
MVEDPIPLPNASMEVSYQNPIEAATIPVQIAVAEPVATPNPPPCLHENKFLVSVEVCLKPSSTARLEDVQRAVERMLENRSMSYADGLVLIPADDLFLVDNVQRICICDTEEWVKNNDVLLFWQVKPVVHTFQLIEEGPCEDLCADGQPASFNEWILPAKEFDGLWESLIYESGLKQRLLRYAASALLFTQKGVNPNLVSWNRIILLHGPPGTGKTSLCKALAQKLSIRCNSRYPHCQLIEVNAHSLFSKWFSESGKLVAKLFQKIQEMVEEDGNLVFVLIDEVESLAAARKAALSGSEPSDSIRVVNALLTQMDKLKSAPNVIILTTSNITTAIDVAFVDRADIKAYVGPPTLHVRYEILRSCVEELISKGIISSFQGCDGLSIPSFSSLKEKLSESEVHDTNTVPWFCKQLIEAAKGCEGLSGRSLRKLPFLAHAALADPYSHDPSNFLCTMIETAKREKSEQPE
Protein: RING-type domain-containing protein (Q38BL9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTTELNSFRVRKSEGVEGEEEDPALTELVFKKLRQTFLCPICHRPLQENPTALDVCGHVFCHSCIVNAIEKSCPSVKDPWEEDERQLTENSHGDQWSSPQKRNSRGRGNINDVRTSPVAKSGRGRSTKRLRLGQSCPICSVPAQISDLISVSLVSNLVSDIMKHPLLSAALVSPKSNDDNDLVKAGHIEEEEALAPSAEVSQVLSTLSGVSLTGNAGVQTVTLQSNNAPPVAEEATGEPEKKSEHGTHRQAIGSLPYSPSATPMGTSPLSVTSHVSVNTTNPHSTVTLSDHNFPVSVRSRSGSPEVVGGVHQTMPEPHGRSKTRGVGCSSPSEVCRPLTSNGDAENSDVLRNFEELSSSCSESGSSQDLQRHSEPCHRTNAVGSGTAGGDALTAVATAVPTSVQSSASTRHFSQKPQEDVGVIDNVGGDALTPVATAVSTSVQSNTLPKDAPTVREVGEGDGKDSSSDSSLSSSDSSSFFGESFNFRVHAQRSEIPTESALIFETKGRANTHENQVHNGGVAVTQNLSSCDPDICSGRELLNHGKNIAGGSGARERSTSTISTSQLSEHKDDVFRLPHTFSVDASVENSTKTGEVLVSAAQMFGARVLDERMGSVDSRLRIYDPKPQKVIRHVFRLPSCQGSGTPAESQLYWKERHYAAASITCSYCLIMPTEGRLASISDDGSCISDCGGVPSARDSNLTSMTPTTACALVSGALVTDFRWIVESVAARCLLPALQYSKRPSWSRHESVSTCGGSGASVDNQTPGRWAAEGHAFMLLPDSVLQLLLQQQTSGSISMRGSSRELSATVTGGYDFCSWRRLILLSGGVLLRFPEECVRQLLLDAMSMSYNDVMIGRNGCDHDERVTAVQNAMHMANGAGRSVFNVECCPERCTASTFLIRNVIILRDSVSTGKDAPCSGSQLLFKRRLERILQSFSVLLSLVQSREVTPVRDVSPSQVFVGSKPFVTFGDVTERYSAPHVMLRSTKWLLRTFSGRLQDSSCESCVGSDQ
Protein: Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 (ACDS complex subunit alpha 1) (EC 1.2.7.4) (ACDS complex carbon monoxide dehydrogenase subunit alpha 1) (ACDS CODH subunit alpha 1) (Q08368)
Organism: Methanosarcina thermophila
Function: Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.
Interaction partners:
Sequence:
MSKLTTGSFSIEDLESVQITINNVIGAAKEAADEKAKDLGPMGPSAWPGLATYRDDWNLKLLDRYEPVITPMCDQCCYCTYGPCDLSNNKRGACGIDMLGHNGREFFLRVITGTACHAAHGRHLLDHLIEVFGEDLPLKLGQSDVLTPNITITTGQRPMTLGEIKPAMEHTEEQLTQLLATVHAGQESAEIDYDSKALFSGSLDHVGMEISDIVQIAALDFPKADPEAPLIEMGVGTIDKEKPFLCVIGHNVGGVTYMMDYMEEHDLTGKMELGGLCCTAIDLTRYKEADRRAPYTKVIGSMSQELKIIRSGLPDVIVVDEQCVRGDIVPEAQKLGIPVIASNAKIMYGLPNRDEQDVDATIEELKSGAIPGAVILDYDKLGEISVRLTQEMHPLREAAGLRKIASDEQMKEWVDKCADCGSCYLVCPEELEIPEAMKHAKEGDYSYLVDLHDQCIGCRRCEQVCKKEIPILSVIEKASQKVIAEEKGWMRAGRGQVSDAEIRAEGLNLVMGTTPGIIAIIGCPNYGDGAKSVYYIAEEFLKRNFIVVGTGCGAMDMGMYKDENGQTLYERFPGGFQSGGLVNIGSCVSNAHITGAAQKVAGIFGGRTMEGNLAEIADYVLNRVGACGLAWGAFSQKASSIGTGCNIYGIPAVLGPHSSKYRRALISKNYDDEKWKVYDARSGEEMAIPPAPEFLLITAETWQEAIPMMAKACIRPSDNSMGRSIKLTHWMELHQKYIGGMPEDWWKFIRTEADLPLAKRAELMKKLEEEHGWEIDWKRKKIISGPKIKFDVSAQPTNLKRLCKGA
Protein: CDC42 small effector protein 2 (Small effector of CDC42 protein 2) (Q9NRR3)
Organism: Homo sapiens (Human)
Function: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages.
Subcellular location: Cytoplasm, cytoskeleton. Cell membrane; Lipid-anchor. Cell projection, phagocytic cup. Note=Recruited to the activated TCR prior actin polymerization. Localizes at the phagocytic cup of macrophages.
Interaction partners:
- Cell division control protein 42 homolog
Sequence:
MSEFWLCFNCCIAEQPQPKRRRRIDRSMIGEPTNFVHTAHVGSGDLFSGMNSVSSIQNQMQSKGGYGGGMPANVQMQLVDTKAG
Protein: N-terminal EF-hand calcium-binding protein 3 (Amyloid-beta A4 protein-binding family A member 2-binding protein) (Nek2-interacting protein 1) (Neuronal calcium-binding protein 3) (X11L-binding protein 51) (Q96P71)
Organism: Homo sapiens (Human)
Function: Inhibits the interaction of APBA2 with amyloid-beta precursor protein (APP), and hence allows formation of amyloid-beta. May enhance the activity of HIF1A and thus promote glycolysis under normoxic conditions; the function requires its ABM domain and may implicate the stabilization of the interaction between HIF1AN and APBA3.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:10833507, ECO:0000269|PubMed:14697346, ECO:0000269|PubMed:26948053}.
Interaction partners:
- Amyloid-beta A4 precursor protein-binding family A member 2
- N-terminal EF-hand calcium-binding protein 2
- N-terminal EF-hand calcium-binding protein 1
- Serine/threonine-protein kinase Nek2
- Amyloid-beta A4 precursor protein-binding family A member 3
Sequence:
MACAGLLTVCLLRPPAPQPQPQTPRHPQLAPDPGPAGHTLFQDVFRRADKNDDGKLSFEEFQNYFADGVLSLGELQELFSGIDGHLTDNLETEKLCDYFSEHLGVYRPVLAALESLNRAVLAAMDATKLEYERASKVDQFVTRFLLRETVSQLQALQSSLEGASDTLEAQAHGWRSDAESVEAQSRLCGSRRAGRRALRSVSRSSTWSPGSSDTGRSSEAEMQWRLQVNRLQELIDQLECKVRAVGPGPHKGGPSWYPPEPGPCWRPGPHSVPSQAPRLEPLREEDLAKGPDLHILMAQRQVQVAEEGLQDFHRALRCYVDFTGAQSHCLHVSAQKMLDGASFTLYEFWQDEASWRRHQQSPGSKAFQRILIDHLRAPDTLTTVFFPASWWIMNNN
Protein: Sorting nexin-27 (Q3UHD6)
Organism: Mus musculus (Mouse)
Function: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes.
Subcellular location: Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Localizes to immunological synapse in T-cells. In T-cells, recruited from the cytosol to sorting endosomes by phosphoinositide-3-kinase products (By similarity). {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 26A
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-1
- Vacuolar protein sorting-associated protein 26B
- Sorting nexin-5
- Sorting nexin-3
- Sorting nexin-6
- Ubiquitin thioesterase otulin
Sequence:
MADEDGEGIHPSAPHRNGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNGVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPTYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGTTVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFALFEVINHSFVRKLAPNEFPHKLYVQNYTSAVPGTCLTIRKWLFTTEEEVLLNDNDLAVTYFFHQAVDDVKKGYIKAEEKSYQLQKLHEQRKMVMYLNMLRTCEGYNEIIFPHCACDSRRKGHVITAISITHFKLHACTEEGQLENQVIAFEWDEMQRWDTDEEGMAFCFEYARGEKKPRWVKIFTPYFNYMHECFERVFCELKWRKENIFQMARSQQRDVAT
Protein: Phosphate-sensing transcription factor (A0A1D8PMD1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MDQQVWNPIFSPSGTTPGKSPSYYNELAPQSQSHISNQDPQLPLQTQHHRLFHIDGGSNHSTPSGNIQLPSSSQQNTPHIVSNTPTAFADSDQVFLQHMEMYDNQQHTNQSAGNTPGPISFHNHNPNLQQASQQPHQHISPHLNNQQQHSQQPYQHQHCHSRSHIDSEAPSANDTPTSSGALGMAPQPPLLSSTTNPQSFDLGLDTIGFIIPEELNFDTDPNHISSAFPPQLPADQTPSLLAVDKLKQLQQQQQQQQRQQDPLSELSSPVLPGQNDQSYNPHHYYHRQSSSNSVFVAGKNTGSSVSAPSQHVRPDAVFTPLVSPVVAPLDTNGKADKENGNNSGGHNNSHSSSFSPQPAVQISFEPLTSPALNAEPSTIKSKGGKKNHKETDDRRRSTSSAYAPSKDENKQYKRRTPHGTPILQGHTSNATTVNGSGKPYKSPITKNGKNSQKQDFSFTNQFEKLPESTITVKSEPMETSVEPPLAPQGQQQDDSNPMLPPNGKPVEITGAPLMGFTMGKLAEGGAGTVADKKSAKKAGANNGKLSRKPSYSKNRNSVSSSSDESSSTSASTSPKMLANNGTNSSGKRSEKPATKKASHKLAEQGRRNRMNNAVQELGRLIPQSYHDEVSIPSKATTVELASKYITALLKEVEELKGRK
Protein: Cytochrome b5 domain-containing protein 1 (Q38CH5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
Sequence:
MPRYYTPHEVRAHCFEDDAYVSINGKVLDITPLIQMYQGTRYASLLQPLILAAGTDMTHLLDKKTMDFKTCIDPETGFRTYAQPFGRFAHTPTVLPDSSIDLSYEVPWWQDERYVIGQLTRKTRKIRIVNTLNGHEHTLEVCSEETLREIVMTRYLSHNAHALSYTWRRLDSEPRDLDMDKTLDENGVLDESEEFESLGLNADYYIPALHLYYDDDLTEA
Protein: Flagellar assembly protein FliH (P31068)
Organism: Escherichia coli (strain K12)
Function: Needed for flagellar regrowth and assembly.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Flagellar hook-length control protein
- Flagellum-specific ATP synthase
- Flagellar biosynthesis protein FlhA
- Flagellar M-ring protein
- Flagellar protein FliO
- Flagellar biosynthetic protein FliP
- Flagellar motor switch protein FliN
- Flagellar motor switch protein FliG
- Flagellar FliJ protein
- Flagellar motor switch protein FliM
Sequence:
MSDNLPWKTWTPDDLAPPQAEFVPIVEPEETIIEEAEPSLEQQLAQLQMQAHEQGYQAGIAEGRQQGHKQGYQEGLAQGLEQGLAEAKSQQAPIHARMQQLVSEFQTTLDALDSVIASRLMQMALEAARQVIGQTPTVDNSALIKQIQQLLQQEPLFSGKPQLRVHPDDLQRVDDMLGATLSLHGWRLRGDPTLHPGGCKVSADEGDLDASVATRWQELCRLAAPGVV
Protein: Reticulon-like protein B3 (AtRTNLB3) (Q9SH59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:17660356}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Reticulon-like protein B18
- Reticulon-like protein B21
- Neurofilament heavy protein
- AT3g15480/MJK13_14
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1
- Reticulon-like protein B17
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
- Arabinogalactan-protein family
- Style cell-cycle inhibitor 1
Sequence:
MAEEHKHEESIMEKISEKIHGHDDSSSSSSDSDDDKNSASLKTKIYRLFGREQPLHKLFGGGKPADIFLWRNKKVSGGVLGAATVSWILFELLEYNLLTLFGHISILALAVLFLWSSASTFIHKSPLHIPEVHIPEDVVLQLASGLRIEINRGFTVLRDIASGRDLKKFLLVIAGLWVLSKVGSSCNFLTLIYIATVLLFTIPVLYEKYEDKVDDFGEKAMREIKKQYVEFDVKVLSKVMSKIPKGAFAFIKKKD
Protein: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1) (P0C344)
Organism: Oryza sativa (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MIIDRVQVEAINSFSNLELLKEVYGLIWILPILTLLLGITIEVLVIVWLEREISASIQQRIGPEYAGPLGLLQAIADGTKLLFKEDILPSRGDIPLFSIGPSIAVISILLSFLVIPLGYRFVLADLSIGVFLWIAISSIAPIGLLMAGYSSNNKYSFLGGLRAAAQSISYEIPLTFCVLAISLLSNSLSTVDIVEAQSKYGFFGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKYGLFYLVSYLNLLVSSLFVTVLYLGGWNLSIPYISFFGFFQMNKMVGILEMTMSIFITLTKAYLFLFISITIRWTLPRMRMDQLLNLGWKFLLPISLGNLLLTTSFQLVSL
Protein: Transforming acidic coiled-coil protein, isoform L (Transforming acidic coiled-coil protein, isoform N) (A0A0B4K6I7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGNKPGKTRKPRALSGKITIKADDGRGNRLSPLAVKPSPKPTSMDQQKAMAAALGHQTAVPGGLKPEDDLVPKFGGLPEFDETQIPELAPLSTDMDTQLKSNHSDSDVFVECLSLHSERYTGDRSELEAYSSALNDVLEQQLSMTSVSTLGAEFNDPLAVSQHNNVSYEAMDVDDLNETMEMLKDVLNAEDRHLMQTHILSVTQSKPENNFVHYHPNQEQNRVELDQLAKHSKPNSDAKESESLVESVLSEESGTQSFEPKLTLSALDSTKDLAKHQEEMQTNTKDIFQKEKHHPVSSAQVKDAQNPKEPEKALNLKEASSELSTKSAKSLEYPNQEKQFSVAVESMERPCTAISLEQNASPAMEATEDRTVEELDQMDVDESMKVDDATVLNSCRQEQINAHSPVSSKFFLKLCVQNDTDCQDNKMDQKTAGKESALKMTEIELPVESVPSASLSPPTPALQAKIIELSLSPPIPTHRPKTAEELEFLALRELPLPDGVSTAGKVECKQLSHGLVPIVAVLPTPLYLDLKGNTTTASLPEPTSPSFPIKEPAEKQSHFPRSPRAQLEQKDMPYLEEAVVERSSHRKQSDFGVIAKSPIVFELTQPSPEKQHLNETLPMSEISPTSSNMTFDSGSITEDKSQKGTENIEPSSTLAVSLGSVDDKQRRTFSVVQPTKEEEEAKSRRTFCMENENPRRTFCMQQNASPAVEATEDTGADEVMDVDISMRADEVAVMKSHQQTWKERQAPISNSPPIPTHQRLNRPPEAISPVSPLGNGTVVLEEQTLSAKEQATLSASDEKDDVFLEHFGAISPVSDDMFKTSSASNNQAKFRVNADEETGGKGASAMIRKRSGTAGEQEEIFDAEFHDGVNNQNLILNSSDFDYLYTKGSNSVPIDRSSLLLKFDPLLGAPVPVNHPNQQEQALQNILGSNQHQNRLLSPTLEEHETSDGNQSFGVISSAKDTAKKWDFKPPVDRTKKHVKMSVDVIDNDCNKTFDNSNTNTEDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKKLDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELIYGKGQGGSS
Protein: RNA-binding protein Nova-1 (Neuro-oncological ventral antigen 1) (Onconeural ventral antigen 1) (Paraneoplastic Ri antigen) (Ventral neuron-specific protein 1) (P51513)
Organism: Homo sapiens (Human)
Function: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons. Binding to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly and exon inclusion. Binding to 5'-YCAY-3' clusters results in a local and asymmetric action to regulate spliceosome assembly and alternative splicing in neurons. Binding to an exonic 5'-YCAY-3' cluster changed the protein complexes assembled on pre-mRNA, blocking U1 snRNP (small nuclear ribonucleoprotein) binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhanced spliceosome assembly and exon inclusion. With NOVA1, they perform unique biological functions in different brain areas and cell types. Autoregulates its own expression by acting as a splicing repressor. Acts to activate the inclusion of exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-2 subunit via a distal downstream UCAU-rich intronic splicing enhancer. Acts to regulate a novel glycine receptor alpha-2 chain splice variant (alpha-2N) in developing spinal cord (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9JKN6}.
Interaction partners:
- Polypyrimidine tract-binding protein 2
- Glycine receptor subunit alpha-2
- Protein FAM107B
- E3 ubiquitin-protein ligase UBR5
- Neurexin-3
- RNA-binding protein Nova-2
- Polypyrimidine tract-binding protein 1
- Gamma-aminobutyric acid receptor subunit gamma-2
- Neurexin-2
- ELAV-like protein 4
Sequence:
MMAAAPIQQNGTHTGVPIDLDPPDSRKRPLEAPPEAGSTKRTNTGEDGQYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLIQGTVEALNAVHGFIAEKIREMPQNVAKTEPVSILQPQTTVNPDRIKQTLPSSPTTTKSSPSDPMTTSRANQVKIIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPDGINLQERVVTVSGEPEQNRKAVELIIQKIQEDPQSGSCLNISYANVTGPVANSNPTGSPYANTAEVLPTAAAAAGLLGHANLAGVAAFPAVLSGFTGNDLVAITSALNTLASYGYNLNTLGLGLSQAAATGALAAAAASANPAAAAANLLATYASEASASGSTAGGTAGTFALGSLAAATAATNGYFGAASPLAASAILGTEKSTDGSKDVVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFVPGTRNRKVTITGTPAATQAAQYLITQRITYEQGVRAANPQKVG
Protein: Solute carrier family 15 member 3 (Solute carrier family 15, member 3, isoform CRA_a) (F5H1C8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPAPRAREQPRVPGERQPLLPRGARGPRRWRRAAGAAVLLVEMLERAAFFGVTANLVLYLNSTNFNWTGEQATRAALVFLGASYLLAPVGGWLADVYLGRYRAVALSLLLYLAASGLLPATAFPDGRSSFCGEMPASPLGPACPSAGCPRSSPSPYCAPVLYAGLLLLGLAASSVRSNLTSFGADQVMDLGRDATRRFFNWFYWSINLGAVLSLLVVAFIQQNISFLLGYSIPVGCVGLAFFIFLFATPVFITKPPMGSQVSSMLKLALQNCCPQLWQRHSARDRQCARVLADERSPQPGASPQEDIANFQVLVKILPVMVTLVPYWMVYFQMQSTYVLQGLHLHIPNIFPANPANISVALRAQGSSYTESWRWSAYTTSTTTRPCPSRLGRSCTTRHHCPSGGRSLSTCSLGSVRSLPASQAWSLPTQRPRAPCRAPSWASSSACRGWAHCWAPA
Protein: Epidermal growth factor receptor pathway substrate 15 (A0A8I6ALY1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLVACAQNGLEVSLSSLNLAVPPPRFHDSSSPLLTSGTSVAELPWAVKSEDKAKYDAIFDSLSPVDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKRKTWVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALAFHLINQKLIKGIDPPHSLTPEMIPPSDKSSLQKNTIGSSPVADFSAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSNWCSSPQSILVNGAADYCSLSTSSSETANLNEHAEGQNNLESEPIHPESSVRSSPEIAPSDVTDESEVVTAADIEKVSPRFDDDKHSKEVNIIVHSVEDPFNVESNPFGGDPFKGSDPFASDCFFKQTSTDPFATSSTDPFSASSNSSNTSVETWKHNDPFAPGGTVVAATDSATDPFASVFGNESFGDGFADFSTLSKVSNEDPFNPTISSSASSVVIPKPVLEETPSKSEDVPPALPPKTGTPTRPCPPPPGKRPINKLDSSDPFKLNDPFQPFPGNDSPKEKDPDMFCDPFTSSSTTANKEAEPSNFANFSAYPSEEDMIEWAKRESEREEEQRLARLNQQEQEDLELAIALSKSEISEA
Protein: Echinus (EC 3.1.2.15) (O77283)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDTAAIKTSLPHAPLAGQQQPQQAQTTTAMAVAPTTITNAQTSAINAKNNIGAFFQTCKVLWHLDAFRRSFRGLNQHVCGGQDCIFCALKELFQQLQTSSEPALCPEPLRRALASGPLAGRRFPLGCLGDAAECFELLLHRVHSHISPDDGDSCESSACIAHRRFAMRVIEQSVCKCGANSEQLPFTQMVHYVSASALTSQKSLALQSHQQLSFGQLLRAAGNMGDIRDCPNTCGAKIGICRALLNRPEVVSIGIVWDSERPAADQVHAVLKAVGTSLRLGDVFHQVSEPRWAQQTQHELVGIVSYYGKHYTTFFFHTKLKVWVYFDDANVKEVGPSWEGVVDKCSRGRYQPLLLLYAVPQQPTVGNGVGIGHVDVAMPASAPSIAGSVVRRAVTPSPEKPSLGNTRRAITPTPLRTPPNDYQNLSVIQKNIFPSNLAMGTDETDAYISRKTVEHVLSAQYQNLSVIQDKIGGGNGVGVGQQSVDKDGGFLSRKPIEAVLSAQLARRQHLQLQRSHSAESSSGHASSNGSSPPSDGLTMPEHLNQPRRRDSGNWSGDRNSASSASSTTLDNPYLYMVAKRGVAAVPQSPTRHGLPYDPGYDSFSLSSTDSYPPKHALNPQLAKIPEAAMGVVPNGGAMPHGHGNGQLALSGDCEKLCHEADQLLEKSRLVEESHDLETALVLCNAAAGRARAAMDAPYSNPHTMTFARMKHNTCVMRARSLHRRILVEKGAETEAMPELKHMREGSTSSVKHVRQNSKDRTLEKEQQQLQFQQIQQIQQIHQIQQQIPASIEIYATLPKRKSPLKALASASACDDNAIEYEQEKQLATSPGKPERESRSLFGRKDKEKEKRSRSEDRNKLTREFSLTETLLVNAKDTLKKHKEDKDEKKEKDKSGKKQHKIRRKLLMGGLIRRKNRSMPDLTEAVDDSTANAGITHHPHYPAQGVTTAGTLLGTSVDDSAVGLGKHGHGMSGYISEGHFDYSGSGSASNSGAGSNPNPNLERSKLMRKSFHGSGRQLTMVPKVAPPPPMRTSSTLTPQQQQQQQQQFHHEANLSNLSAMSSNTSISEDSCQTIITTCAQVHSEQSPLKDLQMLVAQDELPLPPPMELPPYPSPPHSSCHSRQASEDFPPPPPPELDLEPLNQQLSQLQALEAASKQQRQQLESLEGTTSILAQLQQRQHLLKLRKEQANHPGAATTDATWLKELQAKQANDLRAMQRKLEASSPSSVRDLTHRFEQTSIRSYASQELLSQPGQSQQLGQLRTQMNGLPNGNAKMDVDEVDAMPAVRNSLPAALSAHQLLPKPKYEMTQSQIAEEIREVELLNTMVQQTLNQNGAAALPKRVKKKSVSFCDQVILVATAGNEEDDDFIPNPILERVLRTAQHPNEKVTAQMIQQQQQNMMRLQTEAQPRQQQVQQLQQPSPMLGRPAGATADMQRYVQRMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHQELYRQQQLHRTSMSGIASQQHLQQLDAQYTTMPRPLHHSQLGSYSVTLQKHQQLQQQQQQQQQQQAPQQLSLGYFSNGSVATSEQVPLPSPYQRVPLPHGYQPAAAGPYYPLPNAQQHLQQQQLMAKPVQKKVSFEPGTKGEADCLPPPPPPPQKNGLPETGSAGSGHPGAAPGASGAGGTTSAGITAIPTRVYNNAIVKASAKAVECNLCRKRHVIAPAVYCTNCEYYLQMLNQRR
Protein: Sin3A associated protein 130 (H7BXF5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSQQFPRLGAPSTGLSQAPSQIANSGSAGLINPAATVNDESGRDSEVSAREHMSSSSSLQSREEKQEPVVVRPYPQVQMLSTHHAVASATPVAVTAPPAHLTPAVPLSFSEGLMKPPPKPTMPSRPIAPAPPSTLSLPPKVPGQVTVTMESSIPQASAIPVATISGQQGHPSNLHHIMTTNVQMSIIRSNAPGPPLHIGASHLPRGAAAAAVMSSSKVTTVLRPTSQLPNAATAQPAVQHIIHQPIQSRPPVTTSNAIPPAVVATVSATRAQSPVITTTAAHATDSALSRPTLSIQHPPSAAISIQRPAQSRDVTTRITLPSHPALGTPKQQLHTMAQKTIFSTGTPVAAATVAPILATNTIPSATTAGSVSHTQAPTSTIVTMTVPSHSSHATAVTTSNIPVAKVVPQQITHTSPRIQPDYPAERSSLIPISGHRASPNPVAMETRSDNRPSVPVQFQYFLPTYPPSAYPLAAHTYTPITSSVSTIRQYPVSAQAPNSAITAQTGVGVASTVHLNPMQLMTVDASHARHIQGIQPAPISTQGIQPAPIGTPGIQPAPLGTQGIHSATPINTQGLQPAPMGTQQPQPEGKTSVVLADGATIVANPISNPFSAAPAATTVVQTHSQSASTNAPAQGSSPRPSILRKKPATDGMAVRKTLIPPQPPDVASPRVESSMRSTSGSPRPAGAKPKSEIHVSMATPVTVSMETVSNQNNDQPTIAVPPTAQQPPPTIPTMIAAASPPSQPAVALSTIPGAVPITPPITTIAAAPPPSVTVGGSLSSVLGPPVPEIKVKEEVEPMDIMRPVSAVPPLATNTVSPSLALLANNLSMPTSDLPPGASPRKKPRKQQHVISTEEGDMMETNSTDDEKSTAKSLLVKAEKRKSPPKEYIDEEGVRYVPVRPRPPITLLRHYRNPWKAAYHHFQRYSDVRVKEEKKAMLQEIANQKGVSCRAQGWKVHLCAAQLLQLTNLEHDVYERLTNLQEGIIPKKKAATDDDLHRINELIQGNMQRCKLVMDQISEARDSMLKVLDHKDRVLKLLNKNGTVKKVSKLKRKEKV
Protein: Copal-8-ol diphosphate hydratase, chloroplastic (EC 4.2.1.133) (Copal-8-ol diphosphate synthase) (CcCLS) (E2IHE0)
Organism: Cistus creticus subsp. creticus (Rock rose)
Function: Involved in the biosynthesis of oxygen-containing labdane-type diterpenes that may be implicated in direct and indirect defense mechanisms. No activity with geranyl diphosphate or farnesyl diphosphate as substrate.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MAFTFTSAHLFLPVTENHSVHVNYSIPPGNWRLWSTAKGGSNKLDIRRLRCSARRTPEPLAQGSNGGRDGVEAIQRLQTIADDKIDGGANELGIVVWDLIRDGVDAVKSMFDSMGDGDISISAYDTAWVALVKDVNGSGGPQFPSSLQWIVDNQLPDGSWGDSEVFSAYDRLLKTLACVVALKSWNIRPDKCQKGLKFFRDNISKLEKENVEASAQMLSGFEVVFLSLIEVARRLDIQIPLHSPVFEDLIARRNLKFAKIPLDLMHNVPTSLLNSLEGMTGVELDWEKLLKLQSQDGSFITSPSSTAFALMQTNDTKCLGYLKFVVQKFNGGAPGQYPVEIFERIWVVDRLQRLGISRYFQLEIKECCLDYAFKHWTQYGSSWARNTPVYDLDDTCMAFRILRLHGYDVSAEAFRHFEKNGVFFCFGWETTQSVTVNFNLYRATQVAFPGENILKEAKQFSFNFLMKKQAAREFQDKWVILKDFPGELKYALEFPWYASLPRVETRFYVEQYGGDNDVWIGKTLYRMPYINNNVYLELAKLDFNNCQALHRKEWETMQKWFMESKLDEFGVSSKTLLESYFLAAASIFEPERSTERLAWAKTAFLMETIGSYFDDEMNSKDLRKAFVQEFKNIYERRMEAKGTKWNLIIILLTTLNHLTEVCGRDINSYLCHSWEKWMMMWEPEGDRYKGAAELLSNSINLSSGRLFSNDTLSHPNYEKLVTLSNKLCHQLGNSRRGNHNEDSDIKDTKIEIAMQELVQLVHQNSSDDISMDLKQTFFAVVRSFYYAAHCDRGTINSHIVKVLFESVV