wanglab/gogpt-training-data huggingface dataset:
Protein: Protein EXORDIUM-like 4 (Q9FY71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in a brassinosteroid-dependent regulation of growth and development.
Subcellular location: Secreted. Secreted, extracellular space. Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Protein BONZAI 2
- Aluminum induced protein with YGL and LRDR motifs
Sequence:
MAYNYRFAILLVLLSATVGFTAAALKPPVRTLNGNITLNLIWYGKFTPIQRSIIVDFIRSISSVTAAKGPSVASWWKTTEKYKTGVSTLVVGKQLLLENYPLGKSLKSPYLRALSSKLNAGGARSITVVLTAKDVTVEGLCMNRCGTHGSKSSSVNSGAYVWVGNSETQCPGYCAWPFHQPIYGPQSPPLVAPNGDVGVDGMIINIATLLVNTVTNPSPEAVSACTGIFGSGAYPGYAGRVLVDKTSGASYNALGLAGRKYLLPALWDPQTSTCKTMV
Protein: 6-phosphogluconate dehydrogenase, decarboxylating 3, chloroplastic (EC 1.1.1.44) (Q9FFR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:26941195}. Cytoplasm, cytosol {ECO:0000269|PubMed:26941195}.
Interaction partners:
- Probable 6-phosphogluconolactonase 2
- Probable 6-phosphogluconolactonase 1
- Probable 6-phosphogluconolactonase 5
- Probable 6-phosphogluconolactonase 4
- 6-phosphogluconolactonase 3, chloroplastic
- Ribulose-5-phosphate-3-epimerase, chloroplastic
- Probable ribose-5-phosphate isomerase 3, chloroplastic
- Ribulose-phosphate 3-epimerase
- Probable ribose-5-phosphate isomerase 1
- Ribulose-phosphate 3-epimerase
Sequence:
MESVALSRIGLAGLAVMGQNLALNIADKGFPISVYNRTTSKVDETLDRASNEGKLPVAGQYSPRDFVLSIQRPRSVIILVKAGAPVDQTISALSEYMEPGDCIIDGGNEWYQNTERRIVEAEKKGLLYLGMGVSGGEEGARNGPSLMPGGSFTAYNNVKDILEKVAAQVEDGPCVTYIGEGGSGNFVKMVHNGIEYGDMQLISEAYDVLKNVGGLSNDELAEIFTEWNRGELESFLVEITSDIFRVKDDYGDGELVDKILDKTGMKGTGKWTVQQAAELSVAAPTIAASLDCRYLSGLKDERENAAKVLEEAGLKEDIGSASRGVDKKRLIDDVRQALYASKICSYAQGMNLLRAKSLEKGWDLNLGEMARIWKGGCIIRAVFLDRIKKAYQRNPNLASLVVDPDFAKEMVQRQAAWRRVVGLAISAGISTPGMCASLAYFDTYRRARLPANLVQAQRDLFGAHTYERTDRPGAYHTEWTKLARKSQ
Protein: C9orf61 protein (Q8WU02)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MNRRMVGPDVIPLPHIYGARIKGVEVFCPLDPPPPYEAVVSQMDQEQGSSFQMSEGSEAAVIPLDLGCTQVTQDGDIPNIPAEENASTSTPSSTLVRPIRSRRALPPLRTRSKSDPVLHPSEERDNGPIAAQHIQGPQAALAETAWPAAPPELRRPSHLHTSGEAPSREEAPASGG
Protein: CurK (Q6DNE2)
Organism: Lyngbya majuscula
Interaction partners:
Sequence:
MELSSQTTQLSNQQLLLLKIQQATAKLHEIETAATEPIAVIGIGCRFPGGVDSPETYWKLLQEARDLRTEIPKDRWDVDLYYDSDPDVPNKIYVRQGYFLQQPVDQFEPEFFGISGTEAANMDASQRLLLEVTWEALENAGISPKSLKNTDTGVYVGQMTNDYAVIGTNRPDKLPDFYLGIGSNMGMSAGRIAYILGLQGPTLFLDTSCSSSLVALHLACQSLRSRESNLSLVGGVNLMLAPNTTHVLCKGKALSPDSRCKTFDASADGFARGEGCGIVVLKRLRDALADSDRILALVKGSAINHDGPSSGFTVPNQQAQKKVIHQALNNAKVNPLQISYVECHGTGTSLGDPLEVRALDEVYCQQRTKEQLLFLGAVKSNIGHLEAAAGIAALIKVVLALQHQEIPANLHFNQPNPRINWEQIPVKVPTKAFPWLKGEKPRLAGISGFGMSGTNAHVILEEAPIPVKSKSSRATGGQKQVLKDSKGAKLKREEYLERSLHLLTLSAKTQTALDELVSSYENYLKAHPELGVADICYTANTGRTHFNHKLAVVASNQQELVDKLRQQQEGEEVVGIYSGDLPNNSTVPEIALLFTGQGSQYVNMGRQLYQQAPTFREAINQCEEILSSLETFPNKLLQEILYPADDLSDSSLLDQTAYTQPALFAIEYALFKLWQSWGIKPDVVMGHSVGEYVAATVAGVFSLEAGLKLIAARGSLMQKLPAGGAMVSVMASKSKVLETLKAMSRSEKVAIAAINGPQSIVISGEAEAVEAIATHLESVGIKTKQLQVSHAFHSPLMEPMLAEFEDIANQLTYNQPRIPLISNVTGTKADNNIVTGKYWVNHVRQPVQFVQSMKTLHQEGYELFLEIGPKPILLGMGRQCLPEEMGVWLPSLRPGVDEWQQMLSSLGQLYVQGAKVDWFKFDQNYNREKVILPTYPFQRERYWVETQNGYQPKPYGSTAKNLHPLLGEKLNLARIENQHHFQSYLTAESPAYLSQHQVFNKVLFPATGYLEIAAAVGKNLLTTGEQVVVSDVTIVRGLVIPETDIKTVQTVISTLENNSYKLEIFSTSEGDNQQANQWTLHAEGKIFLDSTTNTKAKIDLEQYQRECSQVIDIQQHYQQFKSRGIDYGNSFQGIKQLWKGQGKALGKIALPEEIAGQATDYQLHPALLDAALQILGHAIGNTETDDKAYLPVGIDKLKQYRQTITQVWAIVEIPENTLKGSIKLVDNQGSLLAEIEGLRVTATTADALLKSLQPDISHWFYQINWQTQPLPSTTPSSATDKWLVFAQDTQLVEALQRKSHESIRVSPGDTYKKLTQQHYQINPTSREQFQQLLAENSGITRIVYLWGVQESESKDNLEIQTVQEQSCATVLHLVQAIINSKPETIPKLWLVTRGTQRVISDSEVINPEYGSLWGLGRVIAQEHPELGCKRLDCDPNLEQTQILDSLVAELLSEDVEDQIAIRQGSRYVARLVQKPQQKPITSADQPVQLKLSEYGVIDNLNWQPMQRKTPLANEVEIEVAAVGLNFRDVLNALGLLKDYYAEHFNITSAEQLTFGFECAGKISAVGEQVSQWQVGDEVIGLLLHDGLSSFITTSVEYVVAKPKQMSFSEAATLPLTFLTAQYGLQHLAKIQPGERVLIHAAAGGVGQAAVQIAQVAGAEIFATASPSKWEFLQSLGIKHIMNSRTLDFAEEIMKRTAGEGVDVVLNSLNGEYIPQSLAVLTPKGRFVEIGKIGIWEKEQVKEKRPDVSYFPFDLQEAVQQQPGLIGQLSEELTQQWNQGKLKALPHKVFPSTEITAAFRYMQQAKHVGKVVVSMPEAQSEPKSITADASYLITGGLGALGLEVAQWMVTQGARNIVLTGRRAPKETAQKIIEELETAGASVSVLLGDVSQREDLAKIFQQIQASLPPLKGVIHSAGVLDDALVQNMSWSQFTKVMAPKVQGTWYLHQLTKDFPLDFFVCFSSIASMLGSPGQSNYAAGNGFMDALAHYRRSMGLPGLSINWGAWASAGMAASLAVQNQQRMESMGLSAIEPERGMQALGSLLSESQSQVGVFPVNWSQFIRQFPGGQKIPFLSDFISQTPSLTQKSAFREELEAALVSDRHELLTTHLRLAIAKTLGWKDTQKIGMRQPLFDLGLDSLTAVELKNRLESSLGTSLSSTLLFDYPTVEALVEYLANDVMPIDFSSHLDQTEKALDEEDVVADGSSQLSDITELSEIELEASVLQEIEALEKLI
Protein: Calreticulin (P93508)
Organism: Ricinus communis (Castor bean)
Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
Sequence:
MANPKSLSLFLLSLLAIASAEVFFEERFEDGWENRWVKSDWKKDENTAGEWNYTSGKWNGDPNDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSSSTDQKKFGGDTPYSIMFGPDICGYSTKKVHAILNYNDTNHLIKKEVPCETDQLTHVYTLVIRPDATYSILIDNVEKQTGSLYTDWDLLPPKKIKDPEAKKPEDWDEKEYIPDPEDKKPEGYDDIPKEIPDPDAKKPEDWDDEEDGEWTAPTIANPEYKGPWKPKKIKNPNYKGKWKAPMIDNPDFKDDPEIYVYPNLKYVGIELWQVKSGTLFDNVLICNDPEYAKQLAEETWGKNKDAEKAAFEEAEKKKEEEESKDDPADSDADEDDDDADDTEGEDDGESKSDAAEDSAEDVHDEL
Protein: Uncoordinated 115b, isoform F (A0A126GUR5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNLMSGSTNRSSPFVFVPFSPQTGKQKIYCAKCTKKCSGEVLRVADNHFHKACFQCCQCKKSLATGGFFTKDNAYYCIPDYQRLYGTKCANCQQYVEGEVVSTMGKTYHQKCFTCSKCKQPFKSGSKVTNTGKEVLCEQCVTGAPVSPSRQATGGGVSSPAPPAESPTRATAHQQHGSVISHKAHLKEDYDPNDCAGCGELLKEGQALVALDRQWHVSCFRCKACQAVLNGEYMGKDAVPYCEKCYQKGFGVKCAYCSRFISGKVLQAGDNHHFHPTCARCTKCGDPFGDGEEMYLQGSAIWHPRCGPGPSESGIILNGGGGTSSVVGGASNGNFTDTECDRMSSSALSEMHYRTVSPGLILREYGRPNAEDISRIYTYSYLTDAPHYLRKPIDPYDKTPLSPHFHRPSSYATTASNAGSVAGSRPPSRPHSRTRSAMKVLVDAIRSETPRPKSPGMNNEEPIELSHYPAAKKPPPGEQPKIERDDFPAPPYPYTDPERRRRYSDTYKGVPASDDEDENVENGKPNGKVKNGEEQQRLQREAEQLEKLNSGIGSAIAKDLKEHAKYRKWKQNNLDPRNASRTPSASKEPLYKLRYESPIGASPSRNLDHQKPFYEDEMFDRSTSYRGSLGKSLGNAPSYNVVSALRHVPKPGYGLAPRSHTFSSTTSAAATMHGATDFSYGGLGDKTHSTDLSCGKSEASVDSITEGDRRALMGGDLPASSTYSGALSYHYPQAGLIRRSLPNMSHSIISCANAKL
Protein: Ran GTPase activating protein 1 (B0QYT4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASEDIAKLAETLAKTQVAGGQLSFKGKSLKLNTAEDAKDVIKEIEDFDSLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRTEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVQGFE
Protein: RNA binding protein (O15759)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MAPKSAAKPAASGKNAPAPKSAPAAKSAPATKASAPKNDPKKNAPKAAAPKPAATAPKAAAAKEAKARPAAGTHNGVYVKNWGQGSVTDATRIFSAAGKVVSAQIRRRRYAIIFFENAAAVRKAIDLFNEKEVLGAKVTVSPAKTSPKPDPHEGSSVVFLSPIFRMSTTNGQIRELFTGMRVLRIRTYRQNYAYVYLDSAAAAQKFVKEKNGTEFRGKKLRVALSTRSLQKEKDRAERANLLSDAHNFKKDAKKDIKRDDKKDPKKDSRRNEKKDAKRK
Protein: Regulator of G-protein signaling 21 (RGS21) (Q2M5E4)
Organism: Homo sapiens (Human)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Guanine nucleotide-binding protein subunit alpha-13
- Rho guanine nucleotide exchange factor 1
- Rho guanine nucleotide exchange factor 11
- Beta-adrenergic receptor kinase 1
- Regulator of G-protein signaling protein-like
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MPVKCCFYRSPTAETMTWSENMDTLLANQAGLDAFRIFLKSEFSEENVEFWLACEDFKKTKNADKIASKAKMIYSEFIEADAPKEINIDFGTRDLISKNIAEPTLKCFDEAQKLIYCLMAKDSFPRFLKSEIYKKLVNSQQVPNHKKWLPFL
Protein: Apoptotic signal-regulating kinase 1, isoform B (EC 2.7.11.25) (Q7KSB7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MREKFLSDMRTARDTYATNGAKLQSILHEMRKRLDDPHVLSGEVVHSFMCSLRDVQDYDAMVRLVNDLKNIPNTRKYVETGNMSFLYAFALNRRNRKGDREKALESSLKALEKKENHFPDMLCLCGRIYKDIFVESDYTDATSLAHAIKWYRQSFEVQPNEYAGINLATLLVIEGKEFTNTEELQHIGMTLNNLIGKKGSLSSLSEYWDVATFFEISVLANDYAKAIQAAECMFKLKPPNWYLKSTIGNISLIHRFRKKPEERQPPIEEQVFQFWMDFFLEATNTEEVKNSIRFPILILEPQKIYMPSYVTINMDADEKSIQIVNICLAHAKNACKKIHDFLFVASKIKSVSLYKRDDRCAYLYVHHNSDDFQIYFPSTERRQKFYDMILEMTADQVVFVNLSNDDANIEYEYDYDEQNRKMVLGKGTYGTVYAARDKQTQVRIAIKEVPEKNSQDVQPLHEEIKLHSQLRHRNIVRYLGSCSENGFFKIFMEQVPGGSLSDLLETKWGPLKDNESTMAFYSKQILEGLKYLHEQDIVHRDIKGDNVLVNTYSGVVKISDFGTSKRLARINPMTETFTGTLQYMAPEVIDQGVRGYGPAADIWSFGCTNVEMATGKPPFIELGSAHAAMFKVGFYKKHPNIPEELSANAKNFILRCFAISVMDRPSASQLLEDPFLQDKPRKVRPALPINTEFGRSISVPADRFVHKTTPPLSYNTTCNTPTTPELDITHSSSVDIDELPSNQFMLERRNSHGFLLSPEIEPSTPSLRTSISETSETDGFYRLKKDSQRRTTLSKVLALDESKICDIWLKKVDADQNSIAIRKSDLEVLIRGLRDYIMNENEKHLEATINELKQKLNNDAVALDHLHLALYSFQDAVVCVLRYHCIKPHWMFALDNLVKRAVQAAVTIFSPELGANLADKDLSGNDDESLRTSLMQKGSTESQEKQSLEKVLPTSNTREGVGLTPAESGGDALSSSMECARILRDIRDNQQKLQRQLLEQQRQSMRALHNISQELAHIYMGGRKRLRRTINGFNKKCHRMSTSVGGTSGVRPNIAGNPRRQLNKHHFGLHEVDEQLEQWLTQQEIDEFSKTLILNEGFTFDDFIYNMEKLDLMRLGLRVGIEVRLWKLIIQERVCTSSDCVDSPPSTYHKPIGGNSSFALIDNNNTLPSPTTTTPGTPGIKTKIKKSESEYDSCSE
Protein: UMP-CMP kinase 2, mitochondrial (EC 2.7.4.14) (Nucleoside-diphosphate kinase) (EC 2.7.4.6) (Thymidylate kinase LPS-inducible member) (TYKi) (Q3U5Q7)
Organism: Mus musculus (Mouse)
Function: May participate in dUTP and dCTP synthesis in mitochondria. Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:36443312}.
Interaction partners:
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- UMP-CMP kinase
- Uridine 5'-monophosphate synthase
- Ribonucleoside-diphosphate reductase large subunit
- Uracil phosphoribosyltransferase homolog
- Adenylate kinase 9
- Cytosolic 5'-nucleotidase 3A
- Deoxycytidine kinase
- Nucleoside diphosphate kinase, mitochondrial
- Cytosolic 5'-nucleotidase 1B
Sequence:
MALISRPRAPLWLGRLSRRLCGRHQACMGTMARPRRFTVELPDCSLTHFVLGDATDHRDARLAELLGPPGRSYALCVPLAPGEGCGPRVQAARVHHRLLQQLRRGPLQRCQLSKLLGYGPGDQAGEAQHGFLLRDPCDHPDTRRDLLQLLGSCQEAARPQLAEFQADSQGLLWQRLWELQGDRQVQVDCACVLPAQEPHLHPLLPDLLNSAVFQDRDAARAVLEECTSFIPEARAVLDLVDQCPKEVQKGKFQVIAIEGLDATGKTTLTQSVSESLKAVLLQSPPPCISQWRKIFDDEPTIIRRAFYSLGNYLVASEIAKESTNFPVIVDRYWHSTATYAIATEVSGGLQYLPPAHHPVYQWPGDLLKPDLVLLLTVNSEERVRRLQGRGQEKTKEEAELEANNVFRQKVEMTYQRMENPSCHLVDASPSRETVLQKVLELIQSSGR
Protein: COP9 signalosome complex subunit 1 (SGN1) (Signalosome subunit 1) (G protein pathway suppressor 1) (GPS-1) (JAB1-containing signalosome subunit 1) (Q99LD4)
Organism: Mus musculus (Mouse)
Function: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17276034}. Nucleus {ECO:0000269|PubMed:17276034}.
Interaction partners:
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 7a
- COP9 signalosome complex subunit 7b
- Ubiquitin-like protein NEDD8
- E3 ubiquitin-protein ligase RBX1
Sequence:
MQIDVDPQEDPQNAPDVNYVVENPTLDLEQYAASYSGLMRIERLQFIADRCPPLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRELQNAPDAIPESGVEPPPLDTAWVEATRKKALLKLEKLDTDLKNYKGNSIKESIRRGHDDLGDHYLDCGDLSNALKCYSRARDYCTSAKHVINMCLNVIKVSVYLQNWSHVLSYVSKAESTPEIAEQRGERDSQTQAILTKLKCAAGLAELAARKYKQAAKCFLLASFDHCDFPELLSPSNVAVYGGLCALATFDRQELQRNVISSSSFKLFLELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIRNRALIQYFSPYVSADMHKMAAAFNTTVAALEDELTQLILEGLINARIDSHSKILYARDVDQRSTTFEKSLLMGKEFQRRAKAMILRAAVLRNQIHVKSPPREGSQGELTPANSQSRMSTNM
Protein: Nodal-related 1 (Nodal-related-2) (Squint) (O13144)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MFSCGLLSVVLALAVGLVSCTGNLAGFQETLRNKMRAAGRNGGGRAGHGRHLTRYPLYMMHLYRTLLTGDEKHFSHENPTLYESDSVLSLVAKSCHQVGDKFAVTFDMSSISASDDVQRAELRIRLPHLRSELEVDIYHASTPECERSPCEEVRVHLGTLNANPINSTFRSSWRIFNITALLKYWLHQSERVPFEEPTQMPPMAEGHKSVHHPTANRVMMVVYSKQNRAKTSTLIRTAEHSKYVALDRAGGGSEPVPRRHRRNHRTDDRVRDAAAGMIPGVSHEGGEKKPLCKKVDMWVDFDQIGWSDWIVYPKRYNAYRCEGSCPTPVDETFTPTNHAYMQSLLKLHHPDRVPCLSCVPTRLAPLSMLYYENGKMVMRHHEGMVVAECGCH
Protein: Lethal(3)malignant brain tumor-like protein 2 (L(3)mbt-like protein 2) (P59178)
Organism: Mus musculus (Mouse)
Function: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27' (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14597177}.
Interaction partners:
- Polycomb group RING finger protein 6
- Chromobox protein homolog 3
- Transcription factor E2F6
- E3 ubiquitin-protein ligase RING2
- YY1-associated factor 2
- E3 ubiquitin-protein ligase RING1
- WD repeat-containing protein 5
- RING1 and YY1-binding protein
- Transcription factor Dp-1
- MAX gene-associated protein
Sequence:
MEKPRGTEEAPSSEPMEEEEEDDLDLFGGYDSFRSYNSSAGSESSSYLEESSEAENEDREAGELPTSPLHLFSSANNRSLDGSGSEPAVCEMCGIVGTREAFFSKTKRFCSVSCSRSYSSNSKKASILARLQGKPPTKKAKVLHKAAWSAKIGAFLHAQGTGQLADGTPTGQDALVLGFDWGKFLKDHSYKAAPVSCFKHVPLYDQWEDVMKGMKVEVLNSDAVLPSRVYWIATVIQAAGYRVLLRYEGFENDASHDFWCNLGTVDVHPIGWCAINSKILVPPRTIHAKFTDWKSYLMKRLVGSRTLPADFHIKMVESMKYPFRQGMRLEVVDKTQVSRTRMAVVDTVIGGRLRLLYEDGDSDDDFWCHMWSPLIHPVGWSRRVGHGIKMSDRRCDMSHHPTFRKIYCDAVPYLFKKVRAVYTEGGWFEEGMKLEAIDPLNLGSICVATICKVLLDGYLMICVDGGPSTDGSDWFCYHASSHAIFPATFCQKNDIELTPPKGYETQPFAWETYLEKTKSKAAPARLFNMDCPNHGFKVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDNEYDQWVDCESPDIYPVGWCELTGYQLQPPVSAEPNTPQKGKDTTKKKKKQFGKKRKRIPSAKTRPLRQGSKKPLLEDNLEALGVSEPVPDDIIAVCVKEEHQDISSLDRSPSPQLPLPIESIKQERNN
Protein: Galanin-like peptide (Q9UBC7)
Organism: Homo sapiens (Human)
Function: Hypothalamic neuropeptide which binds to the G-protein-coupled galanin receptors (GALR1, GALR2 and GALR3). Involved in a large number of putative physiological functions in CNS homeostatic processes, including the regulation of gonadotropin-releasing hormone secretion.
Subcellular location: Secreted.
Interaction partners:
- Galanin receptor type 2
- Galanin receptor type 1
- Serine/threonine-protein kinase A-Raf
- Galanin peptides
- 2-phosphoxylose phosphatase 1
- Galanin receptor type 3
Sequence:
MAPPSVPLVLLLVLLLSLAETPASAPAHRGRGGWTLNSAGYLLGPVLHLPQMGDQDGKRETALEILDLWKAIDGLPYSHPPQPSKRNVMETFAKPEIGDLGMLSMKIPKEEDVLKS
Protein: Macrophage colony-stimulating factor 1 (CSF-1) (MCSF) (Proteoglycan macrophage colony-stimulating factor) (PG-M-CSF) [Cleaved into: Processed macrophage colony-stimulating factor 1; Macrophage colony-stimulating factor 1 43 kDa subunit] (Q8JZQ0)
Organism: Rattus norvegicus (Rat)
Function: Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of pro-inflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed macrophage colony-stimulating factor 1]: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Macrophage colony-stimulating factor 1 receptor
- Interleukin-34
- Mast/stem cell growth factor receptor
- Receptor-type tyrosine-protein kinase FLT3
- Granulocyte-macrophage colony-stimulating factor
- Pro-epidermal growth factor
- Vascular endothelial growth factor receptor 2
- Tumor necrosis factor ligand superfamily member 11
- Pro-epidermal growth factor
- Receptor protein-tyrosine kinase
Sequence:
MTARGAAGRCPSSTWMGSRLLLVCLLVSRSVAEVSEHCSHMIGNGHLQILQQLIDSQMETACLIEYKFVDQEQLDDPVCYLKKAFVLVQVIIEETMRFKDNTPNANATERLQELSMKLNSCFIKDYKEQNEACVQTYKESPLRLLEKIKNFFNETKNFLEKDWNIFSKNCNDSFAKCSSRDVVTKPDCNCLYPKATPSSDLASASPHQPPAPSMAPLADLAWDDSQRTEGSSLLPSDLPLRIEDPGSAKQRPPRSTCQTLESTEQPNHEDPQPHPSAGAPIPGVEDIIESSMGTNWVLEEASGEASEGFLTQERKFSPSNPVGGSIQAETDRPWARSASSPFPKLTEDQQPTNITDTPLTEVNPMRPTGQTLNNTPEKTDGSSTLREDQQEPRSPHFATLNPQRVGNSATPYAKLLPPKSHSWGIVLPLGELEGKKSTRDRRSPAELKGGPASEGAARPVAQSTRDRRSPAELKGGPASEGAARPVARFNSIPLTDTGSSIQDPQTSAFVFWVLGIILVLLAVGGLLFYSWKRRSHRDPRTLDSSVGRPEGSSLAQDEDRQVELPV
Protein: AGAP006348-PA (Q7Q5N3)
Organism: Anopheles gambiae (African malaria mosquito)
Interaction partners:
- AGAP007033-PA
Sequence:
MMSLQACQVVLLLVCVTATVHGAIHEIKQNGNRYKIEKVTDSSLKQALASLRQSAWNVKELDLSGNPLSQISAADLAPFTKLELLNLSSNVLYETLDLESLSTLRTLDLNNNYVQELLVGPSIETLHAANNNISRVSCSRGQGKKNIYLANNKITMLRDLDEGCRSRVQYLDLKLNEIDTVNFAELAASSDTLEHLNLQYNFIYDVKGQVVFAKLKTLDLSSNKLAFMGPEFQSAAGVTWISLRNNKLVLIEKALRFSQNLEHFDLRGNGFHCGTLRDFFSKNQRVQTVAKQTVKKLTGQNEEECTVPTLGHYGAYCCEDLPAPFADRLIALKRKEHALLSGQGSETERLECERENQARQREIDALKEQYRTVIDQVTLRKQAKITLEQKKKALDEQVSNGRRAHAELDGTLQQAVGQIELQHATEEQSPLQLLRAIVKRYEEMYVEQQSVQNNAIRDWDMYQHKETQLAEENARLKKLNGEADLALASANATLQELVVREQNLASQLG
Protein: Serine/threonine-protein kinase prk-2 (EC 2.7.11.1) (PIM-related kinase 2) (Q20443)
Organism: Caenorhabditis elegans
Function: Involved in the negative regulation of synaptic differentiation in PLM neurons.
Interaction partners:
- Single-stranded DNA-binding protein homolog sam-10
- peptidylprolyl isomerase
Sequence:
MKKLASLQFFNLKLLLNGESSRGFSKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQTLSWDALTKNKVQKKTSESSDDHHSETLGDHSETEEDRSPPTSSVSQQPGSADEGVGLSASSSNTHNQKKPNHKEFRMAKTSLLAPPTSIEMKAAVQASKTPTQFNVHTALKNQRQIKKHHSPQPPNSTVLTALRRAMSREAQNRISGVFSQD
Protein: Peptidoglycan hydrolase FlgJ (EC 3.2.1.-) (Muramidase FlgJ) (P75942)
Organism: Escherichia coli (strain K12)
Function: Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space.
Subcellular location: Periplasm {ECO:0000250}.
Interaction partners:
- Flagellar basal-body rod protein FlgF
- Flagellar P-ring protein
- Flagellar basal-body rod protein FlgG
- Flagellar hook-associated protein 1
- Basal-body rod modification protein FlgD
- Flagellar L-ring protein
- Flagellar hook-length control protein
- Flagellar basal body rod protein FlgB
- Flagellar hook protein FlgE
- Flagella basal body P-ring formation protein FlgA
Sequence:
MISDSKLLASAAWDAQSLNELKAKAGEDPAANIRPVARQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQMTAGKGLGLAEMMVKQMTPEQPLPEESTPAAPMKFPLETVVRYQNQALSQLVQKAVPRNYDDSLPGDSKAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLEALSDYVGLLTRNPRYAAVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQMKSISDKVSKTYSMNIDNLF
Protein: Vascular-related unknown protein 2 (Q9C6I7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of plant growth.
Interaction partners:
Sequence:
MENSVNNCVRQRVFSNHQIRMIHEEEDHEESSWIVYFEDIDHDDEMVETEGEMTHYYDNDSSMISDAASPVHTTKINNVVRRKANNINTNPKKRRIIHQHKEEEEEELQKGEEEEEDEEDTASSPSNKTKIFSVLDHANDNTRYGKTMDNVTSEEIGCITETGSKIKEIMNEEFSAELKKRGLCVVPLSMLSNFIA
Protein: BEL1-like homeodomain protein 4 (BEL1-like protein 4) (Protein SAWTOOTH 2) (Q94KL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that establishes leaf shape by repressing growth in specific subdomains of the leaf. Negatively regulates knox homeobox gene KNAT1/BP expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein KNATM
- Homeobox-DDT domain protein RLT1
- At4g32030
- Transcription factor bHLH52
- At4g32050
- DNAJ heat shock N-terminal domain-containing protein
- Ubiquitin domain-containing protein 7SL RNA2
- Protein trichome birefringence-like 37
Sequence:
MGLATTTSSMSQDYHHHQGIFSFSNGFHRSSSTTHQEEVDESAVVSGAQIPVYETAGMLSEMFAYPGGGGGGSGGEILDQSTKQLLEQQNRHNNNNNSTLHMLLPNHHQGFAFTDENTMQPQQQQHFTWPSSSSDHHQNRDMIGTVHVEGGKGLSLSLSSSLAAAKAEEYRSIYCAAVDGTSSSSNASAHHHQFNQFKNLLLENSSSQHHHHQVVGHFGSSSSSPMAASSSIGGIYTLRNSKYTKPAQELLEEFCSVGRGHFKKNKLSRNNSNPNTTGGGGGGGSSSSAGTANDSPPLSPADRIEHQRRKVKLLSMLEEVDRRYNHYCEQMQMVVNSFDQVMGYGAAVPYTTLAQKAMSRHFRCLKDAVAVQLKRSCELLGDKEAAGAASSGLTKGETPRLRLLEQSLRQQRAFHHMGMMEQEAWRPQRGLPERSVNILRAWLFEHFLNPYPSDADKHLLARQTGLSRNQVSNWFINARVRLWKPMVEEMYQQEAKEREEAEEENENQQQQRRQQQTNNNDTKPNNNENNFTVITAQTPTTMTSTHHENDSSFLSSVAAASHGGSDAFTVATCQQDVSDFHVDGDGVNVIRFGTKQTGDVSLTLGLRHSGNIPDKNTSFSVRDFGDF
Protein: Lysophospholipase-like protein 1 (EC 3.1.2.22) (Q3UFF7)
Organism: Mus musculus (Mouse)
Function: Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5VWZ2}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 3B
- 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3
Sequence:
MAAVPSAVHLPRCVVSPTGRHSASLIFLHGSGHSGQGQREWIKHVLNQDLTFQHIKIIYPTAPSRPYTPLKGGLSNVWFDRFKISMDCPEHLESIDSMCQVLSGLIDEEVKTGIQKSRILIGGFSMGGCMAMHLAYRSHPDVAGVFVLSGFLNKASVVYQDLQQGGRMLPELFQCHGSADNLVLHAWGKETNSKLKSLGVSTTFHSLPNLNHELNKTELEKLKSWILTRLPGETDGQSE
Protein: Aquaporin TIP4-1 (Tonoplast intrinsic protein 4-1) (ZmTIP4-1) (ZmTIP4;1) (Q9ATL6)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Tonoplast.
Interaction partners:
Sequence:
MAKLMNKLVDSFEHDEIPDVGCVRAVLAELVLTFLFVFTGVSAAMAAGSDGKPGDAMPMATLAAVAIAHALAAGVLVTAGFHVSGGHLNPAVTVGLMVRGHITKLRAVLYVAAQLLASSAACVLLRFLSGGMVTPVHALGRGISPMQGLVMEVILTFSLLFVTYAMILDPRSQVRAIGPLLTGLIVGANSLAGGNFTGASMNPARSFGPALATGDWTNHWVYWIGPLLGGPLAGFVYESLFLVQKMHEPLLNGEV
Protein: Superoxide dismutase [Fe] (EC 1.15.1.1) (P43312)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Interaction partners:
- Ribonuclease 3
- Rhodanese domain-containing protein
- Endoribonuclease YbeY
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL14
Sequence:
MFTLRELPFAKDSMGDFLSPVAFDFHHGKHHQTYVNNLNNLIKGTDFEKSSLFDILTKSSGGVFNNAAQIYNHDFYWDCLSPKATALSDELKGALEKDFGSLEKFKEDFIKSATTLFGSGWNWAAYNLDTQKIEIIQTSNAQTPVTDKKVPLLVVDVWEHAYYIDHKNARPVYLEKFYGHINWHFVSQCYEWAKKEGLGSVDYYINELVHKKA