wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase PRR2 (EC 2.7.11.1) (Pheromone response regulator 2) (Q12310)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein kinase that functions as regulator in the pheromone-induced mating pathway downstream of mitogen-activated protein kinase (MAPK) FUS3. Diminishes transcriptional induction of genes in response to pheromone signaling.
Interaction partners:
- Non-classical export protein 2 homolog 1
- GTP-binding protein RHO5
Sequence:
MSLSRILRYNQRNNKTTASLTAEHAYSDNWAYSVSLGDPTSVGVNMAAKTGEALNKSYDSVFSSLPVADSVPRTDFTASSRDDENTDVQKLTTSWMEKIDTKMPENISKIDSNIISSPMVSKVEARFIVPKGRLRKNSTDFTSSFSNSLSLPKSYGKLIFFTSKKNSSSTKKNLANDISDNKHNNNSSNTIGHNIPVTTATATCDEIACTSTEHEYNVYEEERMFTTRVYSLEDSVSSLSTNPLDDTYSEAVQVNTRHIEDTESTAHIRKHSYTTSLSSIKRLFKITSFSNNNSNSCDHQESTVADDCAISSSLKETTSSPVSTGSFSLMIENEDSDRDQIIQALYSNIEASTDLVSRKYRDLDVVLGEGSGGKVKLVQRVLDNKVFALKEYRSKKKRESERKYIKNIISEYCIASTLKNPNICETLEILYEKGKIFQILEYCEYDLFSLVMSEKMHYEEICCLFKQLINGVKYLHDIGLSHRDLKLDNCVVTRRGILKLIDFGASSVFHYPLSSQMIEANGIVGSDPYLSPEVFYFNEYDPRALDVWSVGIIFFCMITRRFPWKYPKVKDVQFKAFCSGRGVSSFKDLVTRPATDDSNNYDNDGYEEGVIDMGPNFILHRLPEETHKIMRRILEVSPFRRITINGILQDGWIKEIETCQVVGAASPNEASLRIINKGNHIHTNIDQRYAHIGGLHQRT
Protein: RNA N(6)-adenosine-methyltransferase METTL16 (EC 2.1.1.348) (Methyltransferase 10 domain-containing protein) (Methyltransferase-like protein 16) (U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase) (EC 2.1.1.346) (Q86W50)
Organism: Homo sapiens (Human)
Function: RNA N6-methyltransferase that methylates adenosine residues at the N(6) position of a subset of RNAs and is involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts. Able to N6-methylate a subset of mRNAs and U6 small nuclear RNAs (U6 snRNAs). In contrast to the METTL3-METTL14 heterodimer, only able to methylate a limited number of RNAs: requires both a 5'UACAGAGAA-3' nonamer sequence and a specific RNA structure. Plays a key role in S-adenosyl-L-methionine homeostasis by mediating N6-methylation of MAT2A mRNAs, altering splicing of MAT2A transcripts: in presence of S-adenosyl-L-methionine, binds the 3'-UTR region of MAT2A mRNA and specifically N6-methylates the first hairpin of MAT2A mRNA, preventing recognition of their 3'-splice site by U2AF1/U2AF35, thereby inhibiting splicing and protein production of S-adenosylmethionine synthase. In S-adenosyl-L-methionine-limiting conditions, binds the 3'-UTR region of MAT2A mRNA but stalls due to the lack of a methyl donor, preventing N6-methylation and promoting expression of MAT2A. In addition to mRNAs, also able to mediate N6-methylation of U6 small nuclear RNA (U6 snRNA): specifically N6-methylates adenine in position 43 of U6 snRNAs. Also able to bind various lncRNAs, such as 7SK snRNA (7SK RNA) or 7SL RNA. Specifically binds the 3'-end of the MALAT1 long non-coding RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:27872311, ECO:0000269|PubMed:31940410}. Cytoplasm {ECO:0000269|PubMed:31940410}.
Interaction partners:
- Pre-mRNA-splicing regulator WTAP
- Zinc finger CCCH domain-containing protein 13
- Protein virilizer homolog
- RNA-binding protein 15
- N
- N
- Putative RNA-binding protein 15B
- rRNA N
- rRNA N
- E3 ubiquitin-protein ligase Hakai
Sequence:
MALSKSMHARNRYKDKPPDFAYLASKYPDFKQHVQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSIDIPLERLIPTVPLRLNYIHWVEDLIGHQDSDKSTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQNNLSDLIKVVKVPQKTLLMDALKEESEIIYDFCMCNPPFFANQLEAKGVNSRNPRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTYTEFCQGRTMRWALAWSFYDDVTVPSPPSKRRKLEKPRKPITFVVLASVMKELSLKASPLRSETAEGIVVVTTWIEKILTDLKVQHKRVPCGKEEVSLFLTAIENSWIHLRRKKRERVRQLREVPRAPEDVIQALEEKKPTPKESGNSQELARGPQERTPCGPALREGEAAAVEGPCPSQESLSQEENPEPTEDERSEEKGGVEVLESCQGSSNGAQDQEASEQFGSPVAERGKRLPGVAGQYLFKCLINVKKEVDDALVEMHWVEGQNRDLMNQLCTYIRNQIFRLVAVN
Protein: Lipoate-protein ligase A (EC 6.3.1.20) (Lipoate--protein ligase) (P32099)
Organism: Escherichia coli (strain K12)
Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein.
Subcellular location: Cytoplasm.
Interaction partners:
- Lipoyl synthase
- Glycine cleavage system H protein
- Octanoyltransferase
- Probable inner membrane protein Smp
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- 2-oxoglutarate dehydrogenase E1 component
- Dihydrolipoyl dehydrogenase
- Ribose-phosphate pyrophosphokinase
- Glutathione reductase
Sequence:
MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPEQEKELRELSAWMAGAVR
Protein: T. brucei spp.-specific protein (Q4GYA8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHTDDKQAQRYPRTSDAARVHSTLRVGQNTSDKVPYGRLSSQSGPGTPRGDLFPPSNGLSKVEGEETPAAGAWQYPSEPMATPNTRSVQLNGALPVKNEEGETKCSGDAIREEGTKDGGDGVIIGIDAAVEAGVLVANEESGKEDENRESNVNSTPCASGTNETIATATPTLSNATAASVVLTPAVPASTGLRASRRLLDFTGSTNVSNGPRAASRLFDVKPVGGGAQAASQGVGFLRLSKTVPSAASQAVSARMRTSRKNGPTLSATSRGHSSTAHENLPCRNDYTSLRLKEQRRRELYAWNEELRRQDKSDMSADAV
Protein: Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B) (P02638)
Organism: Bos taurus (Bovine)
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 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04271}. Nucleus {ECO:0000250|UniProtKB:P04271}. 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:
- F-actin-capping protein subunit alpha-2
- F-actin-capping protein subunit alpha-1
- Advanced glycosylation end product-specific receptor
- Fibroblast growth factor 2
- Serine/threonine-protein kinase 38
- Glial fibrillary acidic protein
- Protein S100-A1
- non-specific serine/threonine protein kinase
- High mobility group protein B1
- Toll-like receptor 4
Sequence:
MSELEKAVVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDSDGDGECDFQEFMAFVAMITTACHEFFEHE
Protein: Ras association domain-containing protein 6 (Q6ZTQ3)
Organism: Homo sapiens (Human)
Function: Involved in the induction of apoptosis, through both caspase-dependent and caspase-independent pathways. May act as a Ras effector protein. May suppress the serum-induced basal levels of NF-kappa-B (By similarity).
Interaction partners:
- Serine/threonine-protein kinase 3
- Modulator of apoptosis 1
- Ras association domain-containing protein 7
- Serine/threonine-protein kinase 4
- Ras association domain-containing protein 10
Sequence:
MLWEETGAAPAPARASDLPYRISSDHLKKEEKMTMMAHQYPSWIFINEKTFITREQLNSLLKTYNIFYENQKNLHILYGETEDGKLIVEGMLDIFWGVKRPIQLKIQDEKPFSSFTSMKSSDVFSSKGMTRWGEFDDLYRISELDRTQIPMSEKRNSQEDYLSYHSNTLKPHAKDEPDSPVLYRTMSEAALVRKRMKPLMMDRKERQKNRASINGHFYNHETSIFIPAFESETKVRVNSNMRTEEVIKQLLQKFKIENSPQDFALHIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKDAEEISSDVAQYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCLQNKLVIKTETTV
Protein: SCP2 domain-containing protein (Q21481)
Organism: Caenorhabditis elegans
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- MaoC-like domain-containing protein
- Non-specific lipid-transfer protein-like 2
- Acyl-coenzyme A oxidase acox-1.1
- Acyl-coenzyme A oxidase acox-3
- Acyl-coenzyme A oxidase acox-1.3
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase acox-1.4
- Acyl-coenzyme A oxidase acox-1.2
- Probable acyl-coenzyme A oxidase acox-1.5
- Bifunctional glyoxylate cycle protein
Sequence:
MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETVMPQNLVDALKPDYVTPLVTYMVHDSFEESGKVFEAGAGWYGTIQYYKSKGKVISHASADDIAKNWSTITNMNGAEYIGTITEQSARLVSILEEHEASSGSSSASSGASSGGAFPSNIRSSALFQEMADGVKADPTAVKTLKSIVLYIITDGKNELGKFTLDFKSASPSVYLGDVKNGEKANATVTVADSDFVDIAAGKLNAQKAFMSGKLKVKGNVMLLQKLQTVLEKAKKSKL
Protein: Adenosine deaminase domain-containing protein 1 (Testis nuclear RNA-binding protein) (Q5SUE7)
Organism: Mus musculus (Mouse)
Function: Required for male fertility and normal male germ cell differentiation. Plays a role in spermatogenesis. Binds to RNA but not to DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:7543294}.
Interaction partners:
- Bridge-like lipid transfer protein family member 1
Sequence:
MATAGGSRRAPVPGPRLGLPLAAHLPASLGGEGAKDSVGGEKTSGNNDWFQSSRVPSFAQMLKKNLPVQPSAQTVTLPTGYSSESCSLSNMASKVTQVTGNFPEPLLSKGLSSISNPVLPPKKLPKEFIMKYKRGEINPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELLQLDEPEPRVLEPAGPPPIPAEPVVTPEAAYVSKVQYEGRQVQYAKISQLVKETFGQLISNHSQYLKCSSSLAAFIIERAGHHEVVAIGTGEYNYSQCIKPNGRVLHDTHAVVTARRSLLRYFYRQLLLFYSKNPAMMEKSIFCTEPASNLLTLKQNINLYLYMNQLPKGSAQIKSQLRLNPHSISAFEANEELSLHVAVEGKIYLTVYCSADGVNRVNSMSSSDKLTRWEVLGVQGALLSHFIQPVYISSILVGDGNCNDTRGLEIAINQRVDDALTSKLPMFYLVNRPHISLVPTAYPLQINLDHKSLSLNWAQGDNSLEIVDGLNGKITESSPFKSGLSMASRLCKAAMLSRFNLLAKEAKTDDLLEARTYHAAKCMSGPYQEAKALLKAYLQQHGYGSWIVKSPCIEQFSM
Protein: Testicular tissue protein Li 106 (A0A140VJN0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFQAAGAAQATPSHDAKGGGSSTVQRSKSFSLRAQVKETCAACQKTVYPMERLVADKLIFHNSCFCCKHCHTKLSLGSYAALHGEFYCKPHFQQLFKSKGNYDEGFGRKQHKELWAHKEVDPGTKTA
Protein: Major fimbrium tip subunit FimE (B2RH59)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Probably a component of the fimbrium tip; required for incorporation of FimC and FimD into fimbriae. These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in invasion of periodontal tissues and are major virulence factors (Probable). FimC, FimD and FimE contribute to interaction with host CXCR4 and thereby down-regulate the TLR2-mediated host immune response.
Subcellular location: Fimbrium {ECO:0000269|PubMed:17526848}. Cell outer membrane {ECO:0000305}. Note=Probably synthesized as a palmitoylated precursor. Efficient export to the outer membrane and integration into fimbriae requires lipidation and subsequent proteolytic removal of the lipidated propeptide (Probable). Probably part of the fimbrium tip, as a part of the complex formed by FimC, FimD and FimE (PubMed:17675496). {ECO:0000305, ECO:0000305|PubMed:17675496}.
Interaction partners:
Sequence:
MKSKSIIAQLLYVLIAFMAVSCVADKSEPCPSGEPTRVSGSIVSLEHHGLRGASADKENSVERLELWVFDEDGHFLERAVADLSGSTFTAKIIPSEVERRIHFIANYELADPSVWVGRSEREMLPSISVADDLETIRMWARISYPSIAPNQNLGQIQLLRNMAKFSLSVTPPAESKLYDASYALYNSWNKGTLAPFDPNTGSFPQGQITEPAGVVFANPTSEAAFKEADGAHFFYGFERDQSNIGTGAGITCLILKARYNLPNADYTYYKLDFVDTNKVRYNITRNHFYKMILKKAKAPGRPTLQEALDGAAANNIFLSAEVQALPAFSDGSGMLTVDHTYMVFVQGEPSGTFQATYIPQGQNNPDYSKLTVSVSTPTGQQAAVTSAQHEGNGKIKLTLAQQENLTKRSDVVIGVQGNPDLKRSVTVLVREKYQYVFFKANTSSAENNQVTTQISAGQGNELLISAKLPDVLNAALLPITFKVYTEHFYPKTGGMILGIEGGKTLYKYVLTTMPQNKELQFRFKSNKVNSAENIAVKMDYFHDQTIHVTN
Protein: Peptidase C51 domain-containing protein (Q8L1D1)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Subcellular location: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
Interaction partners:
Sequence:
MGATAAKLLIRYRKPIAKAILGFFVFIIVIFLLIFNNDQTAPSGGLATENKNLSESVLRYKSTVEKYARQYDGMEYVPYILALMQIESGGNGGDPMQSSESLGLPPNTIKDPERSIQRGVEFFVENMKSAINRGSDIKTALQAYNYGGGFVDFVVKNGGTYSFELAKQFSINMSGGEKVPYVNALSTTMGYNYRYNYGNMFYVPKLLEYVNESQASAEGVQNNSNNTGAVQVDVPSEYKNKLRYPRYDGHNYNTSGSYPFGQCTWYAFNRMAQIGKPVDDFMGNGGEWGYKGKALGYKVTNKPKVGTAISFPPGSFGSDPVYGHVAFVEVVNADGTLLVSECNVVNPGSGTISYRVVPASIANIASYVE
Protein: Phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) (EC 3.1.4.50) (Glycoprotein phospholipase D) (Glycosyl-phosphatidylinositol-specific phospholipase D) (GPI-PLD) (GPI-specific phospholipase D) (P80108)
Organism: Homo sapiens (Human)
Function: This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.
Subcellular location: Secreted.
Interaction partners:
- Glucosaminyl-phosphatidylinositol-acyltransferase PIGW
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Phospholipase D2
- Phospholipase D1
- Alkaline phosphatase, tissue-nonspecific isozyme
- Phospholipid phosphatase 2
- Phospholipid phosphatase 3
- Phospholipid phosphatase 1
Sequence:
MSAFRLWPGLLIMLGSLCHRGSPCGLSTHVEIGHRALEFLQLHNGRVNYRELLLEHQDAYQAGIVFPDCFYPSICKGGKFHDVSESTHWTPFLNASVHYIRENYPLPWEKDTEKLVAFLFGITSHMAADVSWHSLGLEQGFLRTMGAIDFHGSYSEAHSAGDFGGDVLSQFEFNFNYLARRWYVPVKDLLGIYEKLYGRKVITENVIVDCSHIQFLEMYGEMLAVSKLYPTYSTKSPFLVEQFQEYFLGGLDDMAFWSTNIYHLTSFMLENGTSDCNLPENPLFIACGGQQNHTQGSKMQKNDFHRNLTTSLTESVDRNINYTERGVFFSVNSWTPDSMSFIYKALERNIRTMFIGGSQLSQKHVSSPLASYFLSFPYARLGWAMTSADLNQDGHGDLVVGAPGYSRPGHIHIGRVYLIYGNDLGLPPVDLDLDKEAHRILEGFQPSGRFGSALAVLDFNVDGVPDLAVGAPSVGSEQLTYKGAVYVYFGSKQGGMSSSPNITISCQDIYCNLGWTLLAADVNGDSEPDLVIGSPFAPGGGKQKGIVAAFYSGPSLSDKEKLNVEAANWTVRGEEDFSWFGYSLHGVTVDNRTLLLVGSPTWKNASRLGHLLHIRDEKKSLGRVYGYFPPNGQSWFTISGDKAMGKLGTSLSSGHVLMNGTLKQVLLVGAPTYDDVSKVAFLTVTLHQGGATRMYALTSDAQPLLLSTFSGDRRFSRFGGVLHLSDLDDDGLDEIIMAAPLRIADVTSGLIGGEDGRVYVYNGKETTLGDMTGKCKSWITPCPEEKAQYVLISPEASSRFGSSLITVRSKAKNQVVIAAGRSSLGARLSGALHVYSLGSD
Protein: Protein GAT4 (P40569)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MSTKLPIVISNGTAFKKVPVQLLLNSGSEAQHGLPRNADSQPARPRTGITRTCGQCGEIKTSLQWREGPNGAACLCNACGLFFRKLILRFGRAAAKRYMEQIKGTGTKRRIPKELTGTVRF
Protein: ADAM9 (Q58GH6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGPRALSPLASLRLRWLLACGLLGPVLEAGRPDSEQTVHLSSYEIVTPWRLSRERREALRPSSKQISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDEEGSLLSDHPNVQSHCHYRGYVEGVPNSAVAVSACFGLRGLLHLENASFGIEPLHNSSHFEHVFYPMDDVHQEPLRCGVSNRDTEQEATQGEEEEHPSVTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCAAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGSCLLNIPKPDEAYSAPSCGNKLVDPGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVFIQNGYPCWNSKAYCYNGVCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGVSGSNYKTCATGNALCGKLQCENVQEMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCDAGKICRNFQCVNASVLNYDCDIQGKCHGHGVCNSNKNCHCEDGWAPPHCDTKGYGGSVDSGPTYNAKSTALRDGLLVFFFLIIPLVAAAFFLFIKRDELRKTFRKKRSQMSDGRNQANASRPPGDPSVSRPPGGPSVSRPPGGPNVSRPPGGPNVSRPPGGPSVSRPPPVHGNRFPVPTYAIKQPPQFPSRPPPPQPKIPSQGNLVPARPAPAPPLYSSLT
Protein: Hexosyltransferase (EC 2.4.1.-) (F4IDS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000256|RuleBase:RU362027}; Single-pass type II membrane protein {ECO:0000256|RuleBase:RU362027}.
Interaction partners:
Sequence:
MKQIRRWQRILILALLSISVFAPLIFVSNRLKSITPVGQFRLLSFLFSFHCRREFIEELSKIRFTTNDLRLSAIEHEDGEGLKGPRLILFKDGEFNSSAESDGGNTYKNREEQVIVSQKMTVSSDEKGQILPTVNQLANKTDFKPPLSKGEKNTRVQPDRATDVKTKEIRDKIIQAKAYLNFAPPGSNSQVVKELRGRLKELERSVGDATKDKDLSKGALRRVKPMENVLYKASRVFNNCPAIATKLRAMNYNTEEQVQAQKNQAAYLMQLAARTTPKGLHCLSMRLTSEYFSLDPEKRQMPNQQNYFDANFNHYVVFSDNVLASSVVVNSTISSSKEPERIVFHVVTDSLNYPAISMWFLLNIQSKATIQILNIDDMDVLPRDYDQLLMKQNSNDPRFISTLNHARFYLPDIFPGLNKMVLLDHDVVVQRDLSRLWSIDMKGKVVGAVETCLEGESSFRSMSTFINFSDTWVAGKFSPRACTWAFGMNLIDLEEWRIRKLTSTYIKYFNLGTKRPLWKAGSLPIGWLTFYRQTLALDKRWHVMGLGRESGVKAVDIEQAAVIHYDGVMKPWLDIGKENYKRYWNIHVPYHHTYLQQCNLQA
Protein: Nuclear hormone receptor family member nhr-111 (O45521)
Organism: Caenorhabditis elegans
Function: Orphan nuclear receptor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- HMG box domain-containing protein
- FLYWCH transcription factor 1
Sequence:
MSSQNAKSIGGILETSTVPLVIQPQIVNDPAQNNITLPITLCAVCGDTSNGNHYGVPTCFGCSGFFRRTVRNKLVHGCWNGDGNCVIDKANRNRCKSCRIKKCFKKGMNKNAVQPERTSHSYTVEYVELPSFREYSKGLLPTHSDRLRFQHEHAQHEIDTSSVLVHLKNALQWVQQFSLFAVLSDVEKSQIILTQWPHLLCLALFENSEKIFIDEKFAQLAEKFKSLELSAQDYFLLKGIIIFTETKDGTDLKFDRQLDICIGLLNQLHLESSKSKSGRLLFLLGELKSYSTRQLESLLDLKACEIVISFL
Protein: Serine protease HTRA1A (EC 3.4.21.-) (High-temperature requirement A serine peptidase 1A) (Serine protease 11) (Q6GMI0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Serine protease with a variety of targets, including extracellular matrix proteins and proteoglycans. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. Consequently, may regulate many physiological processes. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets (By similarity).
Subcellular location: Secreted {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Also found associated with the plasma membrane. {ECO:0000250}.
Interaction partners:
Sequence:
MILVTLFCICALVTSLQADARLSKRYVIGGCPSHCDKSMCPTMPKDCSTGQVMDHCNCCLVCASGEGEACGGVGKLGDPVCGESLECSVTGGVSYSATVRRRGKQGVCVCKSSDPVCGSDGVSYRDICELKRVSNRAQSLQQPPVLFIQRGACGTSLHDNPNSLRYKYNFIADVVEKIAPAVVHIELYRKMVYSKREMAVASGSGFVVSDDGLIVTNAHVVANKNRVKVELKNGASYDAKIKDVDEKADIALIKIDLPNKLPVLLLGRSADLRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIRQFLAESYDRLARGRGTTKKRYIGVRMMTLTPSLSKELKGRLRDFPDITSGAYVIEVISKTPAAAGGLKEHDVIISINGQRISTATDVSAIIKKESSLRVVVRRGNEDIILTIIPMEIDP
Protein: DMRT-like family B with proline-rich C-terminal 1 isoform 1 (DMRTB1 protein) (I6L9A0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSLAGPPFGAEAAGSGYPGPLDLRRPMRTVPGPLFTDFVRPLNINPDRALGPEYPGGSSMHPYCPFPLGYLDAPPGVPLQQGFRHVSRSQYQGGGLVSEPGGDFQPSYYLPPPPPPLPPLPPLPPQPQFLPPGYLSALHFLPPPPPPPPPSSFSLTVLFDTDKENTDDQDAEVLSGEPSQPSSQEQSD
Protein: Signal peptidase complex subunit 2 (PfSPC25) (Q9NFA0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity). Also, regulatory component of the CSP25-plasmepsin PMV complex which cleaves the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence of several proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12368867}; Multi-pass membrane protein {ECO:0000255}. Note=Partially colocalizes with plasmepsin PMV in the endoplasmic reticulum (PubMed:30127496). Partially colocalizes with SEC11/SPC21 in the endoplasmic reticulum (PubMed:30127496). {ECO:0000269|PubMed:30127496}.
Interaction partners:
Sequence:
MSGNNVQEEDSTFHVSNLYSETEIKKITQDFISEKIREQNFEEIVKYSNIRIFLSLVLIVIGTYCSIFVQYKKNPVIMIQLLVAFFVVSTTLIIFEYFFFDDVFMILRSNNGSLVKLYCRLDVKKSTLILAYKLNKNVFETSFELKRLYNENGYLMKPYAKNVVMNFLSAHGRTLKLKN
Protein: Ion transport peptide, isoform C (Q0E8W5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCSRNIKISVVLFLVLIPIFAALPHNHNLSKRSNFFDLECKGIFNKTMFFRLDRICEDCYQLFRETSIHRLCKANCFVHETFGDCLKVLLIDDEEISQLQHYLKVINGSPYPFHKPIYH
Protein: Fibroblast growth factor 1 (FGF-1) (Acidic fibroblast growth factor) (aFGF) (Endothelial cell growth factor) (ECGF) (Heparin-binding growth factor 1) (HBGF-1) (P05230)
Organism: Homo sapiens (Human)
Function: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1. Can induce angiogenesis.
Subcellular location: Secreted. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytosol. Nucleus. Note=Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1 (By similarity). Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59. {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 4
- Fibroblast growth factor receptor 3
- Fibroblast growth factor-binding protein 1
- Protein S100-A13
- Synaptotagmin-1
- Fibroblast growth factor 2
- Fibroblast growth factor 17
- Acidic fibroblast growth factor intracellular-binding protein
Sequence:
MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD
Protein: Clathrin adapter accessory protein LAA2 (Large adaptin accessory protein 2) (P32788)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:30523155, ECO:0000303|PubMed:17322287}. Note=Localization depends on ADP-ribosylation factor ARF1. {ECO:0000269|PubMed:30523155}.
Interaction partners:
- Outer spore wall protein LDS1
- Protein ECM13
- Peroxisomal membrane protein PEX32
- Probable transporter SEO1
- Pre-mRNA-splicing factor NTR2
Sequence:
MSDRDQIEPVTNALDAESDSSDDFGNFSDASVENDLYNQNSTLTTSSESVVDNCLNKILPKGEFDLEEETIKNDCFKLSKLIEDERPHVIYEQLVQLDPVLQPFIWNKSHIRRNLLHILRLSDNNGSEGVGTKREEEPLNDELFKRICDAVEKNEQTATGLFLRDNFKIDYTPPMTLKSLQKEEEREQEQHIPQLLMADFTSMDEESLRQYHDTLCQSIDFLVSKSRSLKKQQRDLLKDKTTFENVVTNLTGHTQRLQRDEIALYNKKRNKKKRFSWVGY