wanglab/gogpt-training-data huggingface dataset:
Protein: Probable inactive leucine-rich repeat receptor kinase XIAO (G9LZD7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions in the early stages of organ development by regulating cell division rate. Is probably involved in the regulation of a number of cell-cycle genes. May act as regulator of brassinosteroid (BR) signaling and cell-cycle controlling organ growth.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPPPPRLLFLLVMLLVVAAPGAPVFGANAPPEVKAEIDALLMFRSGLRDPYAAMSGWNASSPSAPCSWRGVACAAGTGRVVELALPKLRLSGAISPALSSLVYLEKLSLRSNSLSGTIPASLSRISSLRAVYLQYNSLSGPIPQSFLANLTNLQTFDVSGNLLSGPVPVSFPPSLKYLDLSSNAFSGTIPANVSASATSLQFLNLSFNRLRGTVPASLGTLQDLHYLWLDGNLLEGTIPSALSNCSALLHLSLQGNALRGILPPAVAAIPSLQILSVSRNRLTGAIPAAAFGGVGNSSLRIVQVGGNAFSQVDVPVSLGKDLQVVDLRANKLAGPFPSWLAGAGGLTVLDLSGNAFTGEVPPAVGQLTALQELRLGGNAFTGTVPAEIGRCGALQVLDLEDNRFSGEVPAALGGLRRLREVYLGGNSFSGQIPASLGNLSWLEALSTPGNRLTGDLPSELFVLGNLTFLDLSDNKLAGEIPPSIGNLAALQSLNLSGNSFSGRIPSNIGNLLNLRVLDLSGQKNLSGNLPAELFGLPQLQYVSLAGNSFSGDVPEGFSSLWSLRHLNLSVNSFTGSMPATYGYLPSLQVLSASHNRICGELPVELANCSNLTVLDLRSNQLTGPIPGDFARLGELEELDLSHNQLSRKIPPEISNCSSLVTLKLDDNHLGGEIPASLSNLSKLQTLDLSSNNLTGSIPASLAQIPGMLSLNVSQNELSGEIPAMLGSRFGTPSVFASNPNLCGPPLENECSAYRQHRRRQRLQRLALLIGVVAATVLLLVLFCCCCVYSLLRWRRRFIEKRDGVKKRRRSPGRGSGSSGTSTDSVSQPKLIMFNSRITYADTVEATRQFDEENVLSRGRHGLVFKACYNDGTVLAILRLPSTSSDGAVVIEEGSFRKEAESLGKVKHRNLTVLRGYYAGPPPDVRLLVYDYMPNGNLATLLQEASHQDGHILNWPMRHLIALGVSRGLAFLHQSGVVHGDVKPQNILFDADFEPHLSDFGLEPMVVTAGAAAAAAAASTSATTTVGSLGYVAPDAAAAGQATREGDVYSFGIVLLELLTGRRPGMFAGEDEDIVKWVKRQLQRGAVAELLEPGLLELDPESSEWEEFLLGIKVGLLCTAPDPLDRPAMGDVVFMLEGCRVGPDIPSSADPTSQPSPA
Protein: Transmembrane protein, putative (DUF247) (Q9S7S4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At5g03100
- At4g12735
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Beta-glucosidase 8
- Probable serine/threonine-protein kinase PBL23
- Serine carboxypeptidase-like 20
- Amine oxidase [copper-containing] zeta, peroxisomal
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
Sequence:
MVLVNVHSDGQPIIINKDMLTWYLLSLKLRQKFQTKNQHSEPVQDPNLHGLPEVTRPNQDQNVQNHKQSHSESGKEVVEERPEETTGDSWVISIRDKLEQADRDDDTTIWGKLCIYRVPHYLQENDKKSYFPQTVSLGPYHHGKKRLRPMERHKWRALNKVLKRLKQRIEMYTNAMRELEEKARACYEGPISLSRNEFTEMLVLDGCFVLELFRGTVEGFTEIGYARNDPVFAMRGLMHSIQRDMIMLENQLPLFVLDRLLELQLGTQNQTGIVAHVAVKFFDPLMPTGEALTKPDQSKLMNWLEKSLDTLGDKGELHCLDVFRRSLLQSSPTPNTRSLLKRLTRNTRVVDKRQQQLVHCVTELREAGVKFRKRKTDRFWDIEFKNGYLEIPKLLIHDGTKSLFSNLIAFEQCHIESSNHITSYIIFMDNLINSSEDVSYLHYCGIIEHWLGSDSEVADLFNRLCQEVVFDPKDSHLSRLSGDVNRYYNRKWNVLKATLTHKYFNNPWAYFSFSAAVILLLLTLCQSFYAVYAYYKPNSKL
Protein: WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 2 (Growth and differentiation factor-associated serum protein 1) (GASP-1) (mGASP-1) (Q7TQN3)
Organism: Mus musculus (Mouse)
Function: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease-inhibitor activity (By similarity). Inhibits the biological activity of mature myostatin, but not activin.
Subcellular location: Secreted {ECO:0000269|PubMed:12595574}.
Interaction partners:
- Growth/differentiation factor 8
- Growth/differentiation factor 11
Sequence:
MCAPGYHRFWFHWGLLLLLLLEAPLRGLALPPIRYSHAGICPNDMNPNLWVDAQSTCKRECETDQECETYEKCCPNVCGTKSCVAARYMDVKGKKGPVGMPKEATCDHFMCLQQGSECDIWDGQPVCKCKDRCEKEPSFTCASDGLTYYNRCFMDAEACSKGITLSVVTCRYHFTWPNTSPPPPETTVHPTTASPETLGLDMAAPALLNHPVHQSVTVGETVSFLCDVVGRPRPELTWEKQLEDRENVVMRPNHVRGNVVVTNIAQLVIYNVQPQDAGIYTCTARNVAGVLRADFPLSVVRGGQARATSESSLNGTAFPATECLKPPDSEDCGEEQTRWHFDAQANNCLTFTFGHCHHNLNHFETYEACMLACMSGPLAICSLPALQGPCKAYVPRWAYNSQTGLCQSFVYGGCEGNGNNFESREACEESCPFPRGNQHCRACKPRQKLVTSFCRSDFVILGRVSELTEEQDSGRALVTVDEVLKDEKMGLKFLGREPLEVTLLHVDWTCPCPNVTVGETPLIIMGEVDGGMAMLRPDSFVGASSTRRVRKLREVMYKKTCDVLKDFLGLQ
Protein: D-galactose-binding lectin (GalNAc/Gal-specific lectin) (MTL) (A0A0G2UGT2)
Organism: Mytilus trossulus (Blue mussel)
Function: D-galactose-binding lectin. Binds both alpha and beta anomer of galactose (Gal). Binds strongly to branched beta-Gal-terminated glycans and weakly to unbranched glycans with alpha-Gal on the end of chains. Has strong affinity for both Gal and GalNAc. Binds glycoproteins containing mucin-type chains. Has hemagglutinating activity towards human group A erythrocytes (Ref.2). Has hemagglutinating activity towards rabbit erythrocytes. Agglutinates V.proteolyticus bacteria. Binds strongly to fungi including species from genera Aspergillus, Alternaria, Fusarium and Haematonectria, and to a lesser extent to fungi from genera Trichoderma. Decreases conidia germination and hyphal growth of fungi. At high concentration, stimulates secretion of cytokines TNF-alpha and IFN-gamma from human peripheral blood cells, and at low concentration reduces hyperexpression of cytokine IL-10 in these cells, indicative of immunomodulatory capability. However, has no effect on IL-4 production (Ref.2). Recognizes pathogen-associated molecular patterns (PAMPs) and binds to peptidoglycan from S.aureus, but has only little binding to beta-1,3-glucan from E.gracilis and lipopolysaccharide (LPS) from E.coli. May be involved in innate immunity acting as an antibacterial or antifungal agent recognizing carbohydrate ligands on the surface of pathogens.
Interaction partners:
Sequence:
MTTFLIKHKASGKYFHPKGGTSNPPNGTNLVLHSDIHERMYFQFEVVNERWRYIKHVASEKIVHPFGGKADPLNGTNMVLHQDRHDRALFAMDFFNDNIRHKGGKYIHPKGGSKNPSNGNLTVMHGDEHGAMEFIFVSPKNKDKRVLVYA
Protein: Cysteine-rich receptor-like protein kinase 36 (Cysteine-rich RLK36) (EC 2.7.11.1) (Q9XEC6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Forms a complex with CRK45 that may negatively control abscisic acid (ABA) and osmotic stress signal transduction. Can phosphorylate CRK45 in vitro.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22225700}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ankyrin repeat family protein
- Cysteine-rich receptor-like protein kinase 45
- Probable calcium-binding protein CML47
Sequence:
MERSNLFHIPCFLLLFLLFNINGVHTTFVCGDEDFSPNTSYVENLESLLPSLASNVIRERGFYNVSLDGVYALALCRKHYEVQACRRCVDRASRTLLTQCRGKTEAYHWDSENDANVSCLVRYSNIHRFGKLKLEPIGNVPHSSLDPSSNLTRISQEFAARANRTVEVASTADESSVLKYYGVSSAEFTDTPEVNMLMQCTPDLSSSDCNHCLRENVRYNQEHNWDRVGGTVARPSCYFRWDDYRFAGAFDNLERVPAPPRSPQTRQDYRVKKGRMFQPWSVVVVVFPTGINLAVFVAFVLAYRRMRRRIYTEINKNSDSDGQATLRFDLGMILIATNEFSLENKLGQGGFGSVYKGILPSGQEIAVKRLAGGSGQGELEFKNEVLLLTRLQHRNLVKLLGFCNEGNEEILVYEHVPNSSLDHFIFDEDKRWLLTWDVRYRIIEGVARGLLYLHEDSQLRIIHRDLKASNILLDAEMNPKVADFGMARLFNMDETRGETSRVVGTYGYMAPEYVRHGQFSAKSDVYSFGVMLLEMISGEKNKNFETEGLPAFAWKRWIEGELESIIDPYLNENPRNEIIKLIQIGLLCVQENAAKRPTMNSVITWLARDGTFTIPKPTEAAFVTLPLSVKPENRSMSERKDKDPFSVDEVSITVLYPR
Protein: Ribokinase (RK) (EC 2.7.1.15) (O60116)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable transketolase
- Ribose-5-phosphate isomerase
- Probable phosphoribomutase
- Ribose-phosphate pyrophosphokinase 5
- Ribose-phosphate pyrophosphokinase 2
- Ribose-phosphate pyrophosphokinase 1
- Phosphoglucomutase
- Uncharacterized glutaminase C222.08c
- Probable pyridoxal 5'-phosphate synthase subunit PDX1
Sequence:
MINIVVLGSMNTDLVMRTKICPSGGETIHGEPDGFSTGNGGKGANQAVAVARLSNPADTKVSMLGCVGDDAFGVEMLSGLKKDGVNVDNVKKIENKSTGVAMIIVEETGENRILLSEGANGNVDTAFVKAMEQRISTCNLLIMQLEIPLEAVEIALQIAHKHGVDVLMNPAPAIPLSHDMISYCAYLVPNEHEAAILLNQADSPATLENVDAYASKLLSFGVRKAVIITLGSQGAYYKSANGESALVSACKVKAVDTTAAGDTFIGAFSNSIAHGQPLKDSLEFAAKCSAITVQRKGAASSIPSLLEVDGSFNLKKNT
Protein: ADP-ribosylation factor-binding protein GGA1 (Golgi-localized, gamma ear-containing, ARF-binding protein 1) (Q06336)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in the regulation of membrane traffic through the trans-Golgi network.
Subcellular location: Golgi apparatus, trans-Golgi network.
Interaction partners:
- Mannose 6-phosphate receptor-like protein 1
- ADP-ribosylation factor 1
- ADP-ribosylation factor-binding protein GGA2
- E3 ubiquitin-protein ligase RSP5
- Polyubiquitin
- RQC trigger complex subunit RQT4
- Ubiquitin-ribosomal protein eS31 fusion protein
- ADP-ribosylation factor 2
- RQC trigger complex subunit CUE3
- Nitrogen permease reactivator protein
Sequence:
MPQRIELTSEPVRKPRSTESSLLRKIQRACRSTLPEPDLGLNLDVADYINSKQGATPREAVLAIEKLVNNGDTQAAVFALSLLDVLVKNCGYSIHLQISRKEFLNDLVKRFPEQPPLRYSKVQQMILEAIEEWYQTICKHASYKDDLQYINDMHKLLKYKGYTFPKVGSENLAVLRPNDQLRTPSELQEEQERAQAAKLEELLRSGKPDDLKEANKLMKIMAGFKDDTKVAVKQAINNELNKLKRKADLFNEMLTSADEPDLENEAIQELYGDLKSAQPKFKKLIEEERDDDALVSNLSKFNDLVIQLLKRYKSIKGMKEEELNVPDTNEPAKELNLIDFDDDTTANTPSVTSPSKSLQPFDDLLGDFNKVSLSSPKSPQENDTVVDILGDAHSKSSGIDLLDFDSQPGESKTALSAYSNSIVLPNGLLNSSSNSKEITAQSQRHILNQSDHLRIDYELTRESMTKLRLVIFYSNISSDPITNFALLVASPKGTTLSLQPQSGNMLQSNSRDGIKQIASVEGISVNLGKPIKLKWKANYCTKGDSKEESGTTSLPTI
Protein: Uncharacterized protein, isoform C (Q9VYM7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Meduse
- Cuticular protein 11A
Sequence:
MLSNGSAGVSADVDVAAGGAADCDERTLLLSEEIVVAPLPASAFSAGVAAAAPPTSLPLVHTTTTQQNNNNVNNNNNGSLVVSAKNMANNKSNKNSSKCKNNEASSSNNNNAATAAATTATTTGEEPVTTTITTATTAADDEDISSDLSDKFPRPQKKPGKLSKLGTKSVGLKRVSFGSSKGSMVETLVFETPTPLSEHMESTFGFDAADTAAAAAGQPQLASTLASQQPLAGGYSGDYAKGTMDDSGIEVQEESERSIVRVSIYNSSQPQVICPPAEYLDFPEFNYSSNLLDYNTMATTAAGIQQQQVIGLGAAYDRQQSTDSGWDNPFRPGGDLSREADEIVNMIRGGKPITPTEERTIGNGSAQHADDNCNGGTAIGESVIKSNLSQNLATAQNGTNSHASATADAGAGKAATATELSGGTGNNGVTSLGQVSKQVVPGPTSASHVVIDEKKNKKKGCCVLQ
Protein: M-phase phosphoprotein 6 (H3BSB3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQRGLDSETKKQLEEEEKKIISEEHWSFIIEEQSFLLCEDLLYGRMSFRGFNPEVEKLMLQMNAKHKAEEVEDETVELDVSDEEMARRYETLVGTIGKKFARKRDHANYEEDENGDITPIKAKKMFLKPQD
Protein: CDKN1A interacting zinc finger protein 1 (F5H2X7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYIRQLRAPSHRSPARGPRIAGPRRPQGATMFSQQQQQQLQQQQQQLQQLQQQQLQQQQLQQQQLLQLQQLLQQSPPQAPLPMAVSRGLPPQQPQQPLLNLQGTNSASLLNGSMLQRALLLQQLQGLDQFAMPPATYDTAGLTMPTATLGNLRGYGMASPGLAAPSLTPPQLATPNLQQFFPQATRQSLLGPPPVGVPMNPSQFNLSGRNPQKQARTSSSTTPNRKDSSSQTMPVEDKSDPPEGSEEAAEPRMDTPEDQDLPPCPEDIAKEKRTPAPEPEPCEASELPAKRLRSSEEPTEKEPPGQLQVKAQPQARMTVPKQTQTPDLLPEALEAQVLPRFQPRVLQVQAQVQSQTQPRIPSTDTQVQPKLQKQAQTQTSPEHLVLQQKQVQPQLQQEAEPQKQVQPQVQPQAHSQGPRQVQLQQEAEPLKQVQPQVQPQAHSQPPRQVQLQLQKQVQTQTYPQVHTQAQPSVQPQEHPPAQVSVQPPEQTHEQPHTQPQVSLLAPEQTPVVVHVCGLEMPPDAVEAGGGMEKTLPEPVGTQVSMEEIQNESACGLDVGECENRAREMPGVWGAGGSLKVTILQSSDSRAFSTVPLTPVPRPSDSVSSTPAATSTPSKQALQFFCYICKASCSSQQEFQDHMSEPQHQQRLGEIQHMSQACLLSLLPVPRDVLETEDEEPPPRRWCNTCQLYYMGDLIQHRRTQDHKPPTPRRDVFAHVPVQGWSTARLVTDMIAKQSLRPFCTVCNRYFKTPRKFVEHVKSQGHKDKAKELKSLEKEIAGQDEDHFITVDAVGCFEGDEEEEEDDEDEEEIEVEEELCKQVRSRDISREEWKGSETYSPNTAYGVDFLVPVMGYICRICHKFYHSNSGAQLSHCKSLGHFENLQKYKAAKNPSPTTRPVSRRCAINARNALTALFTSSGRPPSQPNTQDKTPSKVTARPSQPPLPRRSTRLKT
Protein: Mitogen-activated protein kinase 14 (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (L7RSM2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHINQLQQIMRLTGTPPAYLINRMPSHEARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
Protein: Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B) (P04271)
Organism: Homo sapiens (Human)
Function: Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9925766}. Nucleus {ECO:0000269|PubMed:9925766}. Secreted {ECO:0000250|UniProtKB:P50114}. Note=Secretion into the medium is promoted by interaction with isoform CLSTN3beta of CLSTN3. {ECO:0000250|UniProtKB:P50114}.
Interaction partners:
- Advanced glycosylation end product-specific receptor
- F-actin-capping protein subunit alpha-1
- Cellular tumor antigen p53
- F-actin-capping protein subunit alpha-2
- Fibroblast growth factor 2
- Protein S100-A1
- Ribosomal protein S6 kinase alpha-1
- 45 kDa calcium-binding protein
- Glial fibrillary acidic protein
- Microtubule-associated protein tau
Sequence:
MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE
Protein: ADP-ribosylation factor 2-B (AtARF2) (ARF1-like protein U5) (P0DH91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus.
Interaction partners:
- Coatomer subunit gamma
- ARF guanine-nucleotide exchange factor GNL1
- Coatomer subunit delta
- ARF guanine-nucleotide exchange factor GNL2
- Transmembrane emp24 domain-containing protein p24delta5
- Brefeldin A-inhibited guanine nucleotide-exchange protein 4
- Probable ADP-ribosylation factor GTPase-activating protein AGD9
- ADP-ribosylation factor GTPase-activating protein AGD7
- Kinesin-like protein KIN-14E
- Brefeldin A-inhibited guanine nucleotide-exchange protein 3
Sequence:
MGLSFAKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIAGKA
Protein: Glucose-6-phosphatase 3 (G-6-Pase 3) (G6Pase 3) (EC 3.1.3.9) (Ubiquitous glucose-6-phosphatase catalytic subunit-related protein) (glucose-6-phosphatase-beta) (Glc-6-Pase-beta) (Q6NSQ9)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. May form with the glucose-6-phosphate transporter (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose production through glycogenolysis and gluconeogenesis. Probably required for normal neutrophil function.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Hexokinase-4
- Hexokinase-3
- Hexokinase-2
- Hexokinase-1
- Hexokinase HKDC1
- Phosphoglucomutase-1
- Glucose-6-phosphate 1-dehydrogenase 2
- Glucose-6-phosphate 1-dehydrogenase X
- Glucose-6-phosphate isomerase
- GDH/6PGL endoplasmic bifunctional protein
Sequence:
MESTLSAGIIMAEALQNRLPGLENMWLWVTFLGDPKNLFQFCFPAAYYASRRLGISVLWITFIAEWLNLVFKWFLFGDRPFWWVHESGYSTQTPIQIHQFPSSCETGPGSPSGHCMITGAALWPVMTAISSQVASRSRSPWVRVIPGLAYCTFLLAVGLSRVFLLAHFPHQVLGGLIVGAALGWLMSPRVPMERELSFYGLTALALMLGASLMYWTLFTLGLDLSWSINLASKWCERPEWVHMDSRPFASLSRDSGSALGLGIALHTPCYAQIRRAHLGNGQKIACFVLAMGLLVFLEWLGYPPQISLFYIFNFLKYTLWPCLVLALVPWVVHTLSDQEAPPIRSS
Protein: Slowpoke 2, isoform D (A8DY93)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSQNLQVSYTALAMSDDNQTCSYSMPSVASPSLNHRLQRNVNFNEDLNDLAGYPPQQLPTAPAVRRFSKSIFQRPRSMSVWSDISRSSMRLDERVRVEYYVNENTFKERLQLYFIKNQRSSLRIRIADLFLKLLSCVLYIIRVILDKNPTFITCYGCEVGNKTEFIISAKLTEEEFQENPIINWDAILWVNRPTVLWVLQLLLAMVSLTQSLVLTYLGYKGNIWQQILSFHFILELVTTIPFALTIVHPPLRNLFIPIFLNCWLAKRSLENMFNDLHRAMQKSQSALSQQLTILSATLLCLVFTSVCGIQHFQRAGHRHLNLFQSTYYVVVTFSTVGYGDFVPDIWPSQLYMVIMICVALIVLPTQFEQLAFTWMERQKLGGSYSSHRAQSEKHVVVCSTTLHADTIMDFLNEFYAHPLLQDFYVVLLSPMELDTTMRMILQVPIWAQRVIYIQGSCLKDGDLARARMNEAEACFILAARNYADKTAADEHTILRSWAVKDFAPNVPQYVQIFRPEHKLHVKFAEHVVCEDEFKYALLANNCTCPGASTLVTLLLHTSRGQEGQQSPEEWHRLYGKCSGNEIYHIVLGDSRFFGEYEGKSFTYASFHSHRKYGVALVGVRPAELPEFYEETILLNPGPRHIMKKDDTCYYMSITKEENSAFVVNQNQTSDPTAAAKEGSGTGGGGGASSSASHHHTAATANPTTTITTTVQATTTTISTTFTSSTLLSASTTTATINATSTAAAAPPPVPSVCVRVPHSPSYDSGGGTTGTTHLQPYPYPQSYPQPHPPMQTPDSGEFASLFVPSENPTAVIISDSRQNLKDTTVTQTAATITTTTLPPPPQTMGSPSMAGGSGGCGGGGLGLGSAHSMGTSLSITPATLTTTGNHLDVPFANNPNLLSPDVLNQRRGSRRPSILPVPDMFTSSSFSIAGNDDGEEGDESDDEIDDEMPWRSPSEKIACLGGHFPQSRTYSLIMSSSEDSYQRGCSFCSATASASAAAVAVAVAAAPAPAPAPAYPSDSAGESGTNADSAAMPSEEYLPQLRRRVMKKSYSCDSECRSVPGMGMGMAMGVGLGGGTLARLAARRRQLQRCSSCSCSTATTTTTPAVAATTAMAAGSGATAFTSSSSVETRRPVRPVWVYDYSCIVKGFPPVSPFIGVSPTLCYLLKEKKPLCCLQLAQVCEHCSYRNAKEYQWQNKTIILAADYASNGIYNFIIPLRAHFRSKTSLNPIILLLERRPDVAFLDALSYFPLVYWMLGSIDCLDDLLRAGITLAESVVVVNKELSNSAEEDSLSDCNTIVAVQNMFKFFPSIKSITELSQSSNMRFMQFRAHDKYALHLSKMEKREKERGSHISYMFRLPFAAGAVFSASMLDTLLYQAFVKDYVITFVRLLLGIDQAPGSGFLTSMRITKDDMWIRTYGRLYQKLCSTTCEIPIGIYRTQDTSNADTSHVSNSPVERWGPFSAFSRHCVRLRPSYDEETGTPDSTKDSTEMLRGVTYRPPGSATGGASSFRPQPQRQRSVNCLGGCSERKGSSYSINLADEARDNHAQQIERAEIANLVRSRMESLNLPTIDYDDVSEKRNHLSYVIINPSCDLKLEEGDLIYLVRPSPFSAQKTFERHNSRRKSNISFCSNINLGATCGPQMPQMNMNMANTAVGAGSRRGSGIAGLNPMQMQSVQTLAGYGSSSQRCSPPMQQIKSNSLSLPDSPTVVGNQRGRSNSLRIDNDILLRRSSSLRQGLPSVGVSHGRRKSSLEEIGISHFTTLMQATNHSNPIKISLNGSIGMENQISLQVTPPEEPTPMLGVPCMLGGGGGGGINPSGAGSSTGGMLGGGSSLAINTADLGPGPSTSSGASGSLQAQDSLGQQSSQVSSPQHLQGTIV
Protein: Pre-mRNA-splicing factor cwf24 (Complexed with cdc5 protein 24) (Q9P6R8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mRNA splicing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor cwf26
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-splicing factor sap145
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein cdc28
- Pre-mRNA-splicing factor sap114
- Pre-mRNA-splicing factor cwf14
- Pre-mRNA-splicing factor cwf28
- Peptidylprolyl isomerase cyp7
Sequence:
MEQKNLNINQASGSKINTELAVPIFQSRRRHRPRQGLKRKKGFKRDDDSGGSSESSNEDMRDNIPIVSGRKKTVRLNRLQRESEQFENSALKDINVEYQSNLSATGESVNTTTVSAINEDTREVILGRPSPKLANQSTLPTELFQSQNDYSRFLPKRKDFEKKSQVGPVLSSNASTVRMNTIIDYQPDVCKDYKLTGYCGYGDTCKFLHMREDYKAGWQLDREWDSVQEKYKKGAKLEEGMVKNEKKEDIPFVCLICKKDYRSPIATTCGHHFCEQCAITRYRKTPTCIQCGADTKGLFSVDKNFDRLLKNRKSKNDEAVKQKVGGFESNNSATTEVSERKDREASFQGFADTLAKPNTSAQQKMPSLGDNSNTIISKYFIREITESNIVHFKRLVRVVLEASYSDKFYRLVLKNPDYARIATFEDKFVGAISSLVAEDNSLYVTVLCVLAPYRCLGIGSLLIDHVKKTAINNNIDRISLHVQTTNESVIKWYTAHGFKIVKQINDFYRRLENKSAFYMVCPLSAHNNIISNH
Protein: Methyltransferase (A0A076GD02)
Organism: Sinorhizobium phage phiLM21
Interaction partners:
Sequence:
MSQNTSSAVMQQRSEPHDSLDDFPTQPWATRALCDHVLSGCYLPGKTVWEPACNRGHMSAPLAEHFGAVWASDIHDYGTPGSFRHDFLFPVMPLSESPDWIISNPPFRLAEQFIARARELATEGVAMIVRTSFLEGVGRYENLFSKNPPSIVAQFAERVPMVKGRLTATGSTATSYCWLVWLKGVTTTKLVWIPPCRKKLERPDDYSAYREEVAA
Protein: Homeobox protein Hox-B9 (Homeobox protein Hox-2.5) (P20615)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Protein BTG2
- Homeobox protein Hox-B8
- Homeobox protein Hox-B5
- Homeobox protein Hox-B6
- Pre-B-cell leukemia transcription factor 1
Sequence:
MSISGTLSSYYVDSIISHESEDAPPAKFPSGQYANPRQPGHAEHLDFPSCSFQPKAPVFGASWAPLSPHASGSLPSVYHPYLQPQGAPAAESRYLRTWLEPAPRAEAAPGQGQAAVKAEPLLGAPGELLKQGTPEYSLETSAGREAVLSNQRAGYGDNKICEGSEDKERPDQTNPSANWLHARSSRKKRCPYTKYQTLELEKEFLFNMYLTRDRRHEVARLLNLSERQVKIWFQNRRMKMKKMNKEQGKE
Protein: Pituitary adenylate cyclase-activating polypeptide (PACAP) [Cleaved into: PACAP-related peptide (PRP-48); Pituitary adenylate cyclase-activating polypeptide 27 (PACAP-27) (PACAP27); Pituitary adenylate cyclase-activating polypeptide 38 (PACAP-38) (PACAP38)] (P41535)
Organism: Sus scrofa (Pig)
Function: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine secretion (By similarity). Involved in the control of glucose homeostasis, induces insulin secretion by pancreatic beta cells (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Vasoactive intestinal polypeptide receptor 1
- Glucagon-like peptide 1 receptor
- Beta-1 adrenergic receptor
- Thyrotropin receptor
- D
- Guanylate cyclase
- 5-hydroxytryptamine receptor 6
- Adenosine receptor A2
- Follicle-stimulating hormone receptor
Sequence:
MTMCSGARLALLVYGIIMHSSVYCSPAAAGLRFPGIRPEDEAYDEDGNPLQDFYDSDPPGVGGPASTLRDAYALYYPAEERDVAHGILNKAYRKVLDQLSARKYLQTLMAKSVGGNLDGGAEDDSEPLSKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNKGRRIAYL
Protein: Calponin-homology (CH) domain-containing protein (D0IMZ8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAQPKRLDQEEEVVPAIRHDDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISMGWIQEKREDGDNKEETPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMIHPEIDEMSVMTYLSQFPATKPIIMKPKVQATISNLDKILQVNDPREFDLKLSRDGFKPKVSIRDEDGQDIHLSLKKVEDKENAYKVKFTPTKIGFIHVDVAANDVHTFETQTIPEASVICQVVPIARLLDYNKTAKVGDDVKFAVVDAIEGPVEAIVVDPTGKEHRMVILDGTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPFPLRGKPKNSFKVWGRGIAPEGIRKNDVVGVHVESLDPEENIANANISLEVLKPSDGSHLPVSVGYNDESQSMDFEYSPKQAPDDLEVLVKVAGEVIESHKIHVAPESSSKIRAFGAGLEGGIVNEPCVFDVEMNGESKDLSFAVEGPSKAEIGCQERPDGSAILSYTPTVAGVYKVGVLADGKHIQDSPFVLRVTEPIEGLKPSATRVTGIDESKVYNVGEKIPFRVDTRLCGVDLVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAGVSVPGAPFSVKVKEPTDASKLKIFGPGVDGPVYSKEPTRFTIDATQAGPGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVFAGEEISPIEINVKPNVDVSGIRVEGLENENLLIGSHLRPTINIGKLEPKSKGLQLIDEVNGKRYNVPMKINPDGTYSTDTPLMEVGEHKLQLLFDEIPVKEAVVEVIKGTDVNKCKAYGPGLEQAVVGEKAVFELDLDGAGEGALSMEMRGPAKAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGKDEQKEHVKGSPFKAVVDYKKDPSQITISGLDQPNYRLNQPINFVIDTSKTKDLPVKATVPSDFAQLQPVVSRSPSNPRHHNVRFVPSGKPNVSIPIEIIYDGLKIDEKLVKVLPEVEPQLIKILHDKKKDSLTTTPITTNASHEGHVPFDVRDCGNVKKIESRVFGPDGKERLNHVRSTEQNGIYDVSFPTDMAGEYCVVFYINGQEVAARVPVMAEKIGRKEDVIKEEIVFHPEIAEHSPTVLTYNHPIDAKKKKAHPAIQVLAAKPDAVRLEHIQELVDNGHRVADRIVFTATKLGTNTLDVFYGGEHVDHVEYEAIGKLEYERIQAERAKVVVEKEDDVDKYEKQYKFQFNVRDLGYQPKDLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIKFYVDAYGDGWATVYGPGLQNAVVGEPATFTVCAKGSQAKELSVSIEGPAKSQIKIHDNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDSPFRVLVMGEGQKRSHLSVGSTSEVALPITQQELKGISASIKSPGGIEEPCFVRLLDGGRLGVSFTPREAGEHLITVKRDGKLVPKAPFKIKVDKTQVGDASKVEVSGSGKAKGITLQANELLVDTSKAGYGGLSVSVQGPSKAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFADHHVKDSPLTVQCTGKSAGRVIQTIQKDVEQHGICLPDQESHLFLKLLNTSPMDITARLMDPKGHTDDIEMRDLGQQYYQLKFTPKMEGIHTLSVMYKDAHVNGSPFQFTVGSFSEGGAHKVRAAGQGVVRGETGTFNAFNIYHREAGVGAVAVTIEGPSKATLEFKDHNDGNCHVDYKVATPGEYVVAVKFNDQHIPDSPFKVYIAPATGEVRKLELAQFHGQGIPAGKAFTFTVLTHRAKGHLEAKVVTPNNEVDTIDIVPIEDGESYAMRFVPKETGNHFIHVTLDGAPMRESPFRLRVGGKDLCDPTAISASGDGLVKGTTGQKCEFVINTANAGAGILTVQMDGPSKATLDAYELEKGYKVRYTPLAPGSYFASVKYNGIHAPGSPFKIPVEGKELGGNGYNETSHVKIDAVAKTSKGTVAVVPEYQGDAAKVTAKGAGLNKFFPGRPAAFQIDTGLAGTNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGDKEIPGSPFAIEP