wanglab/gogpt-training-data huggingface dataset:
Protein: NCK adaptor protein 1 isoform 3 (A0A0S2Z4E4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS
Protein: Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375) (Q9C0B5)
Organism: Homo sapiens (Human)
Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, fatty acid uptake, bacterial sensing or cardiac functions. Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins. Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2. Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2. Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes. Participates also in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane. Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis. Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26334723, ECO:0000269|PubMed:29185452, ECO:0000269|PubMed:31402609, ECO:0000269|PubMed:32958780}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000269|PubMed:26334723}.
Interaction partners:
- Golgin subfamily A member 7
- Golgin subfamily A member 7B
- Claudin domain-containing protein 1
- Tomoregulin-1
- Palmitoyltransferase ZDHHC3
Sequence:
MPAESGKRFKPSKYVPVSAAAIFLVGATTLFFAFTCPGLSLYVSPAVPIYNAIMFLFVLANFSMATFMDPGIFPRAEEDEDKEDDFRAPLYKTVEIKGIQVRMKWCATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLTAHIMGVFGFGLLYVLYHIEELSGVRTAVTMAVMCVAGLFFIPVAGLTGFHVVLVARGRTTNEQVTGKFRGGVNPFTNGCCNNVSRVLCSSPAPRYLGRPKKEKTIVIRPPFLRPEVSDGQITVKIMDNGIQGELRRTKSKGSLEITESQSADAEPPPPPKPDLSRYTGLRTHLGLATNEDSSLLAKDSPPTPTMYKYRPGYSSSSTSAAMPHSSSAKLSRGDSLKEPTSIAESSRHPSYRSEPSLEPESFRSPTFGKSFHFDPLSSGSRSSSLKSAQGTGFELGQLQSIRSEGTTSTSYKSLANQTRNGSLSYDSLLTPSDSPDFESVQAGPEPDPPLGYTSPFLSARLAQQREAERHPRLVPTGPTHREPSPVRYDNLSRHIVASLQEREKLLRQSPPLPGREEEPGLGDSGIQSTPGSGHAPRTSSSSDDSKRSPLGKTPLGRPAVPRFGKPDGLRGRGVGSPEPGPTAPYLGRSMSYSSQKAQPGVSETEEVALQPLLTPKDEVQLKTTYSKSNGQPKSLGSASPGPGQPPLSSPTRGGVKKVSGVGGTTYEISV
Protein: Probable aquaporin NIP7-1 (NOD26-like intrinsic protein 7-1) (AtNIP7;1) (Q8LAI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ACT domain-containing protein ACR3
- Boron transporter 4
- Probable aquaporin SIP1-2
- Probable aquaporin SIP2-1
- NEP1-interacting protein 2
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- Aquaporin SIP1-1
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
Sequence:
MNGEARSRVVDQEAGSTPSTLRDEDHPSRQRLFGCLPYDIDLNPLRIVMAELVGTFILMFSVCGVISSTQLSGGHVGLLEYAVTAGLSVVVVVYSIGHISGAHLNPSITIAFAVFGGFPWSQVPLYITAQTLGATAATLVGVSVYGVNADIMATKPALSCVSAFFVELIATSIVVFLASALHCGPHQNLGNLTGFVIGTVISLGVLITGPISGGSMNPARSLGPAVVAWDFEDLWIYMTAPVIGAIIGVLTYRSISLKTRPCPSPVSPSVSSLLR
Protein: RNA-binding protein 24-A (RNA-binding motif protein 24-A) (RRM domain-containing protein SEB-4) (SEB-4) (Xseb-4) (Q6GQD3)
Organism: Xenopus laevis (African clawed frog)
Function: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation. Plays a major role in pre-mRNA alternative splicing regulation. Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation. Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing. Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes. Plays a role in the regulation of mRNA stability and mRNA translation to which it is bound. Involved in myogenic differentiation by regulating myog levels. Binds to a huge amount of mRNAs. Required for embryonic heart development, sarcomer and M-band formation in striated muscles.
Subcellular location: Nucleus {ECO:0000269|PubMed:10842088}. Cytoplasm {ECO:0000269|PubMed:10842088}.
Interaction partners:
Sequence:
MHTTQKDTTYTKIFVGGLPYHTTDSSLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQIHPALIQRPFGIPAHYVYPQAYVQPGVVIPHVQPTAATSTSPYIDYTSAAYAQYSAAAAAAAYDQYPYAASPAATGYVTAAGYGYAVPQPLTAAAPGSAAAAAAAFGQYQPQQLQADRMQ
Protein: Alpha-protein kinase 1 (EC 2.7.11.1) (Chromosome 4 kinase) (Lymphocyte alpha-protein kinase) (Q96QP1)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that detects bacterial pathogen-associated molecular pattern metabolites (PAMPs) and initiates an innate immune response, a critical step for pathogen elimination and engagement of adaptive immunity. Specifically recognizes and binds ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria. ADP-Heptose-binding stimulates its kinase activity to phosphorylate and activate TIFA, triggering pro-inflammatory NF-kappa-B signaling. May be involved in monosodium urate monohydrate (MSU)-induced inflammation by mediating phosphorylation of unconventional myosin MYO9A. May also play a role in apical protein transport by mediating phosphorylation of unconventional myosin MYO1A. May play a role in ciliogenesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:30111836}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:30967659}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30967659}. Cell projection, cilium {ECO:0000269|PubMed:30967659}. Note=Localized at the base of primary cilia. {ECO:0000269|PubMed:30967659}.
Interaction partners:
- TRAF-interacting protein with FHA domain-containing protein A
Sequence:
MNNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRALLPSELRTLIQEAKEMKWPFVPEKWQYKQAVGPEDKTNLKDVIGAGLQQLLASLRASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVAKGLHKLQPATPIAPQVVIRQARISVNSGKLLKAEYILSSLISNNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEAAELIWASIVGYLALPQPDKKGLSTSLGILADIFVSMSKNDYEKFKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAYTPLFVLTAVNIRGTCLLSYSSSNDCPPELKNLHLCEAKEAFEIGLLTKRDDEPVTGKQELHSFVKAAFGLTTVHRRLHGETGTVHAASQLCKEAMGKLYNFSTSSRSQDREALSQEVMSVIAQVKEHLQVQSFSNVDDRSYVPESFECRLDKLILHGQGDFQKILDTYSQHHTSVCEVFESDCGNNKNEQKDAKTGVCITALKTEIKNIDTVSTTQEKPHCQRDTGISSSLMGKNVQRELRRGGRRNWTHSDAFRVSLDQDVETETEPSDYSNGEGAVFNKSLSGSQTSSAWSNLSGFSSSASWEEVNYHVDDRSARKEPGKEHLVDTQCSTALSEELENDREGRAMHSLHSQLHDLSLQEPNNDNLEPSQNQPQQQMPLTPFSPHNTPGIFLAPGAGLLEGAPEGIQEVRNMGPRNTSAHSRPSYRSASWSSDSGRPKNMGTHPSVQKEEAFEIIVEFPETNCDVKDRQGKEQGEEISERGAGPTFKASPSWVDPEGETAESTEDAPLDFHRVLHNSLGNISMLPCSSFTPNWPVQNPDSRKSGGPVAEQGIDPDASTVDEEGQLLDSMDVPCTNGHGSHRLCILRQPPGQRAETPNSSVSGNILFPVLSEDCTTTEEGNQPGNMLNCSQNSSSSSVWWLKSPAFSSGSSEGDSPWSYLNSSGSSWVSLPGKMRKEILEARTLQPDDFEKLLAGVRHDWLFQRLENTGVFKPSQLHRAHSALLLKYSKKSELWTAQETIVYLGDYLTVKKKGRQRNAFWVHHLHQEEILGRYVGKDYKEQKGLWHHFTDVERQMTAQHYVTEFNKRLYEQNIPTQIFYIPSTILLILEDKTIKGCISVEPYILGEFVKLSNNTKVVKTEYKATEYGLAYGHFSYEFSNHRDVVVDLQGWVTGNGKGLIYLTDPQIHSVDQKVFTTNFGKRGIFYFFNNQHVECNEICHRLSLTRPSMEKPCT
Protein: Peroxisomal membrane protein PEX16 (A0A0G2JWT6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Peroxisome membrane {ECO:0000256|RuleBase:RU365003}.
Interaction partners:
- Peroxisomal biogenesis factor 19
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX13
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX14
- Peroxisomal ATPase PEX6
- Similar to peroxisome biogenesis factor 26.
- Peroxisome biogenesis factor 10
- Peroxisomal targeting signal 2 receptor
- ATP-binding cassette sub-family D member 3
Sequence:
MEKLRLLGLRYQEYVTRHPAATAQLETAVRGLSYLLAGRFSDSHELSELVYSASNLLVLLNDGILRKELRKKLPVSLSQQKLLTWLSVLECVEVFMEMGAAKVWGEVGRWLVIALIQLAKAVLRMFLLIWFKTGIQTSPPIVPLDRETQAQPLDGDHNLGSPEPSYVGKRSNRVVRTLQNSPSLHSRHWGAPQQREIRQKQQQEELSTPPTPLGLQETIAESLYIARPLLHLLSLGLWGQRSWAPWLLSGVVDMTSLSLLSDRKNLTRRERLELRRRTILLLYYLLRSPFYDRFSEAKILFLLQLLADHIPGIGLVARPLMDYLPSWQKIYFYSWG
Protein: Immunoglobulin superfamily member 11 (IgSF11) (Q5U2P2)
Organism: Rattus norvegicus (Rat)
Function: Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- V-set immunoregulatory receptor
Sequence:
MTRRRSALASWLLLSLLGVAASLEVSESPGSVQVARGQTAVLPCAFSTSAALLNLNVIWMVIPLSNANQPEQVILYQGGQMFDGALRFHGRVGFTGTMPATNVSIFINNTQLSDTGTYQCLVNNLPDRGGRNIGVTGLTVLVPPSAPNCQIQGSQDIGSDVILLCSSEEGIPRPTYLWEKLDNTLKLPPTATQDQVQGTVTIRNISALSSGLYQCVASNAIGTSTCLLDLQVISPQPRSVGVIAGAVGTGAVLIVICLALTSGAFFYWRSKNKEEEEEEIPNEIREDDLPPKCSSAKAFHTEISSSENNTLTSSNTYNSRYWNNNPKPHKNTESFNHFSDLRQSFSGNAVIPSIYANGNHLVLGPHKTLVVTANRGSSPQVMPRNNGSVSRKPWSQHTHSYTVSQMTLERIGAVPVMVPAQSRAGSLV
Protein: Protein RRP5 homolog (NF-kappa-B-binding protein) (NFBP) (Programmed cell death protein 11) (Q14690)
Organism: Homo sapiens (Human)
Function: Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:14624448, ECO:0000269|PubMed:17654514}.
Interaction partners:
- RNA cytidine acetyltransferase
- Nucleolar protein 14
- Nucleolar protein 6
- CCAAT/enhancer-binding protein zeta
- Small subunit processome component 20 homolog
- Ribosome biogenesis protein BMS1 homolog
- WD repeat-containing protein 46
- KRR1 small subunit processome component homolog
- U3 small nucleolar RNA-associated protein 4 homolog
- HEAT repeat-containing protein 1
Sequence:
MANLEESFPRGGTRKIHKPEKAFQQSVEQDNLFDISTEEGSTKRKKSQKGPAKTKKLKIEKRESSKSAREKFEILSVESLCEGMRILGCVKEVNELELVISLPNGLQGFVQVTEICDAYTKKLNEQVTQEQPLKDLLHLPELFSPGMLVRCVVSSLGITDRGKKSVKLSLNPKNVNRVLSAEALKPGMLLTGTVSSLEDHGYLVDIGVDGTRAFLPLLKAQEYIRQKNKGAKLKVGQYLNCIVEKVKGNGGVVSLSVGHSEVSTAIATEQQSWNLNNLLPGLVVKAQVQKVTPFGLTLNFLTFFTGVVDFMHLDPKKAGTYFSNQAVRACILCVHPRTRVVHLSLRPIFLQPGRPLTRLSCQNLGAVLDDVPVQGFFKKAGATFRLKDGVLAYARLSHLSDSKNVFNPEAFKPGNTHKCRIIDYSQMDELALLSLRTSIIEAQYLRYHDIEPGAVVKGTVLTIKSYGMLVKVGEQMRGLVPPMHLADILMKNPEKKYHIGDEVKCRVLLCDPEAKKLMMTLKKTLIESKLPVITCYADAKPGLQTHGFIIRVKDYGCIVKFYNNVQGLVPKHELSTEYIPDPERVFYTGQVVKVVVLNCEPSKERMLLSFKLSSDPEPKKEPAGHSQKKGKAINIGQLVDVKVLEKTKDGLEVAVLPHNIRAFLPTSHLSDHVANGPLLHHWLQAGDILHRVLCLSQSEGRVLLCRKPALVSTVEGGQDPKNFSEIHPGMLLIGFVKSIKDYGVFIQFPSGLSGLAPKAIMSDKFVTSTSDHFVEGQTVAAKVTNVDEEKQRMLLSLRLSDCGLGDLAITSLLLLNQCLEELQGVRSLMSNRDSVLIQTLAEMTPGMFLDLVVQEVLEDGSVVFSGGPVPDLVLKASRYHRAGQEVESGQKKKVVILNVDLLKLEVHVSLHQDLVNRKARKLRKGSEHQAIVQHLEKSFAIASLVETGHLAAFSLTSHLNDTFRFDSEKLQVGQGVSLTLKTTEPGVTGLLLAVEGPAAKRTMRPTQKDSETVDEDEEVDPALTVGTIKKHTLSIGDMVTGTVKSIKPTHVVVTLEDGIIGCIHASHILDDVPEGTSPTTKLKVGKTVTARVIGGRDMKTFKYLPISHPRFVRTIPELSVRPSELEDGHTALNTHSVSPMEKIKQYQAGQTVTCFLKKYNVVKKWLEVEIAPDIRGRIPLLLTSLSFKVLKHPDKKFRVGQALRATVVGPDSSKTLLCLSLTGPHKLEEGEVAMGRVVKVTPNEGLTVSFPFGKIGTVSIFHMSDSYSETPLEDFVPQKVVRCYILSTADNVLTLSLRSSRTNPETKSKVEDPEINSIQDIKEGQLLRGYVGSIQPHGVFFRLGPSVVGLARYSHVSQHSPSKKALYNKHLPEGKLLTARVLRLNHQKNLVELSFLPGDTGKPDVLSASLEGQLTKQEERKTEAEERDQKGEKKNQKRNEKKNQKGQEEVEMPSKEKQQPQKPQAQKRGGRECRESGSEQERVSKKPKKAGLSEEDDSLVDVYYREGKEEAEETNVLPKEKQTKPAEAPRLQLSSGFAWNVGLDSLTPALPPLAESSDSEEDEKPHQATIKKSKKERELEKQKAEKELSRIEEALMDPGRQPESADDFDRLVLSSPNSSILWLQYMAFHLQATEIEKARAVAERALKTISFREEQEKLNVWVALLNLENMYGSQESLTKVFERAVQYNEPLKVFLHLADIYAKSEKFQEAGELYNRMLKRFRQEKAVWIKYGAFLLRRSQAAASHRVLQRALECLPSKEHVDVIAKFAQLEFQLGDAERAKAIFENTLSTYPKRTDVWSVYIDMTIKHGSQKDVRDIFERVIHLSLAPKRMKFFFKRYLDYEKQHGTEKDVQAVKAKALEYVEAKSSVLED
Protein: Vanillin aminotransferase (EC 2.6.1.119) (Putative aminotransferase) (pAMT) (D6R3B6)
Organism: Capsicum frutescens (Cayenne pepper) (Tabasco pepper)
Function: Participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum frutescens. Capsaicinoids, the alkaloids responsible for the heat or pungency of chili pepper, are synthesized from phenylpropanoid intermediates in the placental tissue of chili peper fruit (Probable). Can transfer an amine from alanine to vanillin, forming vanillylamine and pyruvate.
Interaction partners:
Sequence:
MANITNEFMGHDMLAPFTAGWQSDMEPLVIEKSKGSYVYDINGKKYLDTLSGLWCATLGGSETRLVEAANKQLNTLPFYHSFWNRTTKPSLDLAKELLNMFTANKMAKVFFTNSGSEANDTQVKLVWYYNNALGRPQKKKIIARAKAYHGSTYISAGLSGLPPMHQKFDLPPPFVLHTECPHYWAYHLPGETEEEFSTRLANNLESLILNEGPETVAAFIAEPVLGAAGVILPPATYFDKVQAILRKHDILFIADEVVCGFGRLGTMFGSDKYNIKPDLVSVAKALSSGYMPIAAVLVSQKISSVILSESNKIGAFCHGFTYSGHPVACAVALEALKIYKERNITEVVNKISQKFQEGLKAFADSPIIGEIRGTGLALSTEFVDNKSPNDPFPYEWAVGTYFGAQCAKYGMLVSSTGDHVNMAPPFTLSLEELDELIRIYGKALKDTEKRVEELKSQKK
Protein: E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SLX8) (Synthetic lethal of unknown function protein 8) (P40072)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 that mediates ubiquitination and subsequent desumoylation of sumoylated proteins and proteins containing SUMO-like domains for their degradation. The STUbL complex SLX5/SLX8 stimulates ubiquitin conjugating enzymes, including UBC1, UBC4, UBC5 and UBC13-MMS2, and mediates the proteolytic down-regulation of sumoylated proteins. The STUbL complex SLX5/SLX8 is involved in ubiquitin-mediated degradation of histone variant CSE4, preventing mislocalization to euchromatin. The complex plays an essential role in maintenance of chromosome stability and links SUMO-dependent ubiquitination to a centromere-specific function during mitosis. The complex is involved in proteolysis of spindle positioning protein KAR9 and ensures correct spindle function by regulating levels of microtubule-associated proteins. During replication, the complex helps to prevent DNA lesions via recombination and has a role in localizing the DNA damage protein DCD2. The complex especially ubiquitinates the nuclease YEN1 and prevents persistent accumulation of a fraction of YEN1 associated with sites of activity in late G2/M and helps maintain the balance between pro- and anti-crossover pathways during homologous recombination. It is also involved in ubiquitin-mediated degradation of DNA repair proteins RAD52 and RAD57. Finally, the complex is recruited to distinct genomic hotspots of non-H2B protein ubiquitination (ub-hotspots) by the sumoylated transcription factor-like protein EUC1 where it ubiquitinates EUC1 and presumably other targets.
Subcellular location: Nucleus {ECO:0000269|PubMed:17591698, ECO:0000269|PubMed:18948542}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:26906737}. Note=Localizes to few distinct genomic hotspots of non-H2B protein ubiquitination (ub-hotspots). {ECO:0000269|PubMed:31015336}.
Interaction partners:
- E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5
- E3 SUMO-protein ligase SIZ2
- ATP-dependent helicase SGS1
- DNA repair and recombination protein RAD52
- E3 SUMO-protein ligase SIZ1
- SUMO-conjugating enzyme UBC9
- Ubiquitin-conjugating enzyme E2 4
- Ubiquitin-like protein SMT3
- Ubiquitin-like-specific protease 1
- ERAD-associated E3 ubiquitin-protein ligase ASI1
Sequence:
MARRPDNQNPEGENLRIKRVRLESVRQNDEEEENEVSRTQNIVTDNRHDSPEAVVEIIGERALENTSEEDGDDDLSLFRALEEDPGSDHNTSNNDSGNHDRETMHTEEPEASSGNNITLTNNVEELHTMDVLSQTANTPSASPMLDAAPPTTKPGTNSKEQTVDLTADAIDLDAEEQQVLQISDDDFQEETKEAPKEYGAAKDYRCPICFEPPETALMTLCGHVFCCPCLFQMVNSSRTCRQFGHCALCRSKVYLKDVRLIILRKKQVKKKVKS
Protein: Battenin (G3MU35)
Organism: Caenorhabditis elegans
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Lysosome membrane {ECO:0000256|RuleBase:RU361113}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361113}.
Interaction partners:
Sequence:
MIKKEQIVRVPTVAPTHLDSRHCQSISTGAVLLADNLPALVVQTTFPFFMHRFPFGFRAFLVFLLQASSYFVVAYSKNIAMSLAGVCMASLGQGIGEITFLAMAAHYIPETIASWSSGTGGAGLIGSFSYAFITQAGLSPSNTLLVQLFIPVVFAGAYFFLLTIPPTVYSPTIHPSTWIIPKNYDKDVFEAAEARGDVLNTKKVPQRELGPLERIKLIGPLLYLMVPLATVYTAEYMINQGLTELIIFNCSQGLSLPLSSQYRWYQVLYQLGVFISRSSVKFFEMPLWLIWCLPILQCVNMIFFFFEAVYWFTPTIIIIFVLIVFEGLLGGSAYVNTYNKIHKKVNPDVREYSLSAASMGNSLGTNIAAFLSIPLYNWVCTMKAPGR
Protein: CTD small phosphatase-like protein 2 (CTDSP-like 2) (EC 3.1.3.-) (Q05D32)
Organism: Homo sapiens (Human)
Function: Probable phosphatase.
Interaction partners:
- Serine/threonine-protein kinase PDIK1L
Sequence:
MRLRTRKASQQSNQIQTQRTARAKRKYSEVDDSLPSGGEKPSKNETGLLSSIKKFIKGSTPKEERENPSKRSRIERDIDNNLITSTPRAGEKPNKQISRVRRKSQVNGEAGSYEMTNQHVKQNGKLEDNPSSGSPPRTTLLGTIFSPVFNFFSPANKNGTSGSDSPGQAVEAEEIVKQLDMEQVDEITTSTTTSTNGAAYSNQAVQVRPSLNNGLEEAEETVNRDIPPLTAPVTPDSGYSSAHAEATYEEDWEVFDPYYFIKHVPPLTEEQLNRKPALPLKTRSTPEFSLVLDLDETLVHCSLNELEDAALTFPVLFQDVIYQVYVRLRPFFREFLERMSQMYEIILFTASKKVYADKLLNILDPKKQLVRHRLFREHCVCVQGNYIKDLNILGRDLSKTIIIDNSPQAFAYQLSNGIPIESWFMDKNDNELLKLIPFLEKLVELNEDVRPHIRDRFRLHDLLPPD
Protein: 15-cis-phytoene desaturase, chloroplastic/chromoplastic (EC 1.3.5.5) (Phytoene dehydrogenase) (Phytoene desaturase) (Q40406)
Organism: Narcissus pseudonarcissus (Daffodil)
Function: Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:9288918}. Plastid, chromoplast {ECO:0000269|PubMed:29176862, ECO:0000269|PubMed:8653112, ECO:0000269|PubMed:9288918}. Membrane {ECO:0000269|PubMed:8653112, ECO:0000269|PubMed:9288918}; Peripheral membrane protein {ECO:0000250|UniProtKB:A2XDA1}. Note=Exists as an inactive soluble form and an active membrane-bound form. {ECO:0000269|PubMed:8653112}.
Interaction partners:
Sequence:
MSIVGLVSVVCPSGGIKKRYFSKGLDNFQGFRSSECLGIQLQVPVPFYSGIRQSPRATSLQVVCKDCPRPELEGAVNFLEAAQLSASFRSSPRPEKGLEVVVVGAGLAGLSTAKYLADAGHKPILLESRDVLGGKIAAWKDKDGDWYETGLHIFFGAYPNVQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPEVLPAPLNGIWAILRNNEMLTWPEKVRFAIGLLPAMVGGQAYVEAQDGLTVTEWMRRQGVPDRVNDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVDHIQSLGGRAQLNSRLQKIELNPDGTVKHFVLGNGNIITGDAYVVAAPVDILKLLLPQEWREIPYFQKLDKLVGVPVINVHIWFDRKLKNTYDHLLFTRSPLLSVYADMSVTCKEYYDPNRSMLELVFAPAEEWISRSDSEIIERTMKELAKLFPDEIAADQSKAKILKYHVVKTPRSVYKTIPDCEPCRPLQRSPIEGFYLAGDYTNQKYLASMEGAVLSGKLCAQSIVQDYELLVRRSKKASTAEMTVV
Protein: ADP-ribosylation factor-like protein 6-interacting protein 4 (ARL-6-interacting protein 4) (Aip-4) (HSP-975) (HSVI-binding protein) (SR-15) (SRp25) (SR-25) (Splicing factor SRrp37) (Q66PJ3)
Organism: Homo sapiens (Human)
Function: Involved in modulating alternative pre-mRNA splicing with either 5' distal site activation or preferential use of 3' proximal site. In case of infection by Herpes simplex virus (HSVI), may act as a splicing inhibitor of HSVI pre-mRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:19582790}. Nucleus speckle {ECO:0000269|PubMed:19582790}.
Interaction partners:
- Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
Sequence:
MAHVGSRKRSRSRSRSRGRGSEKRKKKSRKDTSRNCSASTSQGRKASTAPGAEASPSPCITERSKQKARRRTRSSSSSSSSSSSSSSSSSSSSSSSSSDGRKKRGKYKDKRRKKKKKRKKLKKKGKEKAEAQQVEALPGPSLDQWHRSAGEEEDGPVLTDEQKSRIQAMKPMTKEEWDARQSIIRKVVDPETGRTRLIKGDGEVLEEIVTKERHREINKQATRGDCLAFQMRAGLLP
Protein: Coilin (A0A8I5ZU31)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAASETVRVRLQFDYPPPATPHCTVFWLLVDLNRCRVVTDLISLIRQRFGFSSGALLGLYLEGGLLPPSESARLVRDNDCLRVKLEDQGLPEALIVSNGGDSNFPCRKSKKRAFKLVEDEETDQGYKYPDKYWKRQEDSGPNEKASDLETKLFPDEVRRTKNKRKSKVAGIPAEEDEEETKKKSSKRKEKCEQKKQTRASKSPKQQTHKEGGSQNCSFPRASYRSSLAKARRRSSTGAKGSPSYLSESESCPDSVSDGHCSVTTMQGVTLSEKLSAELLKDGATKTAAANRQSSKPSFTFSSGKGKASRASSSSSDSSSESEDQFLVSKNMLEGASDFLKTTGLFAGQGCSSPGLSLETPGIMGWKPSDSNRGRQAPGPNVPVPTSLGRGWGRGEDFLFGKGLRGRGIRGRGRGRGQTVSCILNRSSESQKQKQLNDILTNSSTVIQNPVETSKKDYSLLPLLAAAPQVGEKIAFKEGKILSHDPETQQVDIEVLSSLPALKEPGKFDLVYHNENGTEVVEYAVTQEKRITVFWKELIDPRLIIDSSSSISSK
Protein: Uncharacterized protein C17D1.01 (Q10207)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MKAVYLDYLLRIRYTYVFNLKVSYQSERRTYGATEHFVGCLVPKAWNCLADDYTDIKTLLDLLFGVTAVIIFACTFKCFTMTEDGLTKLNLEAFLGVSGNTQELLESLGISAIPDLSNLGASNNNNSGLTFDPNDPSAAAFYIAQQVAAIEHPPPRKMTSSEKTRSENRERKKRWREQNEERNKDNDLRCRVNKKAKKLFGSEPSIEKTNWIEAEFTRRHTKRKEKERACLSQNQSSNASRANSQSLLPDLDLLATNSSANAVLQGSAINNALNALAKDPNLIHSLLTQIDFDPSKSKDGLNLGSLTDVVPPQPPQPEHELAALQEHNEAHDAAMRQYELERQQNAMLPGLASIDGLQALPHLDFSDSAVTNQSHSQSQNSLHPLISQSETHSIFSALSETPTPVSGNGNVADAPPDFSLSQVMPLDLIAPSMQPSAVSSPMSESHVQISSEMPRTGMSALPMRPRSQNVDKHRKFPYYNKRNAVTTPSSPYDGAQSGSPQFPPFELPPHNYSQAQSPNLATPSPSFSSLPDVSLPPIVKPNLMSEPTPTNSDEKSHALGFPPPPGQKIEFQRSSSKNGTAKSD
Protein: Protein sprouty homolog 3 (Spry-3) (Sprouty RTK signaling antagonist 3) (Sprouty3) (O43610)
Organism: Homo sapiens (Human)
Function: Inhibits neurite branching, arbor length and neurite complexity (By similarity). Inhibits EGF-mediated p42/44 ERK signaling (By similarity). Negatively regulates the MAPK cascade, resulting in a reduction of extracellular matrix protein accumulation. May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Vesicle-associated membrane protein 7
- Interleukin-9 receptor
Sequence:
MDAAVTDDFQQILPIEQLRSTHASNDYVERPPAPCKQALSSPSLIVQTHKSDWSLATMPTSLPRSLSQCHQLQPLPQHLSQSSIASSMSHSTTASDQRLLASITPSPSGQSIIRTQPGAGVHPKADGALKGEAEQSAGHPSEHLFICEECGRCKCVPCTAARPLPSCWLCNQRCLCSAESLLDYGTCLCCVKGLFYHCSTDDEDNCADEPCSCGPSSCFVRWAAMSLISLFLPCLCCYLPTRGCLHLCQQGYDSLRRPGCRCKRHTNTVCRKISSGSAPFPKAQEKSV
Protein: protein-secreting ATPase (EC 7.4.2.8) (Q6XVW8)
Organism: Shigella flexneri
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSYIKLLTQLSFPNRISGPILETSLSDVSIGEICNIQAGIESNEIIARAQVVGFHDEKTILSLIGNSRGLSRQTLIKPTAQFLHTQVGRGLLGAVVNPLGEVTDKFAVTDNSEILYRPVDNAPPLYSERAAIEKPFLTGVKVIDSLLTCGEGQRMGIFASAGCGKTFLMNMLIEHSGADIYVIGLIGERGREVTETVDYLKNSEKKSRCVLVYATSDYSSVDRCNAAYIATAIAEFFRTEGHKVALFIDSLTRYARALRDVALAAGESPARRGYPVSVFDSLPRLLERPGKLKAGGSITAFYTVLLEDDDFADPLAEEVRSILDGHIYLSRNLAQKGQFPAIDSLKSISRVFTQVVDEKHRIMATAFRELLSEIEELRTIIDFGEYKPGENASQDKIYNKISVVESFLKQDYRLGFTYEQTMELLGETIR
Protein: Cell cycle regulated microtubule associated protein (Q5XUX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Flowering time control protein FY
- Cleavage stimulation factor subunit 77
- Cleavage stimulating factor 64
- Similarity to unknown protein protein family)
- TPX2
- TPX2
- FIP1[III]-like protein
- FIP1[V]-like protein
- Ribonuclease J
- Cleavage and polyadenylation specificity factor subunit 3-I
Sequence:
MVPESSSRIMSFSGDDFEFDIDFEFDAPRFYDFSRPELYSETEEIEIWFQSSGNYPPSPFSPKFNWKFEPFKQITNTISESKPVEIIESSEAETGLNCKDKFNGFIYYNQTVKDVSKKKSKSKTKTSNSTLTRPTASLLARQNKPLDIYSVQLLTRCQRSLAKFGENVAPVLVSKLQNQDTNRQKQEAKVAHVSSRAKLTVPKEPNLRTAERSERHRSKVNTQREQIATSNSKRHIRNKNINLEPVSTSLAKTNTPRSQHFQAFRLRTSLRAKERSSNAKTDVVQENDATKSRTLKKPIDSLKTRIVKENHSRKINCQVYESKSSPLDPKISSKEDLVEAIRIEYGNQSSCRTDINRSLDLCRKFDSQEVARNLITA