wanglab/gogpt-training-data huggingface dataset:
Protein: Protein kinase C, brain isozyme (PKC) (EC 2.7.11.13) (dPKC53E(BR)) (P05130)
Organism: Drosophila melanogaster (Fruit fly)
Function: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins (By similarity). PKC also serves as the receptor for phorbol esters, a class of tumor promoters (By similarity). Acts in a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required for the activation of Cad99C and consequently Cad99C-dependent endosome formation, which is essential for the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Inactivation-no-after-potential D protein
- Transient receptor potential protein
- Serine/threonine-protein kinase mTor
- Transient receptor potential-gamma protein
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase classes I and II
- Protein kinase C, eye isozyme
- Protein ROP
- PRKCA-binding protein
- Matrix metalloproteinase-2
Sequence:
MSEGSDNNGDPQQQGAEGEAVGENKMKSRLRKGALKKKNVFNVKDHCFIARFFKQPTFCSHCKDFICGYQSGYAWMGFGKQGFQCQVCSYVVHKRCHEYVTFICPGKDKGIDSDSPKTQHNFEPFTYAGPTFCDHCGSLLYGIYHQGLKCSACDMNVHARCKENVPSLCGCDHTERRGRIYLEINVKENLLTVQIKEGRNLIPMDPNGLSDPYVKVKLIPDDKDQSKKKTRTIKACLNPVWNETLTYDLKPEDKDRRILIEVWDWDRTSRNDFMGALSFGISEIIKNPTNGWFKLLTQDEGEYYNVPCADDEQDLLKLKQKPSQKKPMVMRSDTNTHTSSKKDMIRATDFNFIKVLGKGSFGKVLLAERKGSEELYAIKILKKDVIIQDDDVECTMIEKRVLALGEKPPFLVQLHSCFQTMDRLFFVMEYVNGGDLMFQIQQFGKFKEPVAVFYAAEIAAGLFFLHTKGILYRDLKLDNVLLDADGHVKIADFGMCKENIVGDKTTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLYEMLVGQPPFDGEDEEELFAAITDHNVSYPKSLSKEAKEACKGFLTKQPNKRLGCGSSGEEDVRLHPFFRRIDWEKIENREVQPPFKPKIKHRKDVSNFDKQFTSEKTDLTPTDKVFMMNLDQSEFVGFSYMNPEYVFSP
Protein: Ankyrin repeat and SOCS box protein 11 (ASB-11) (Q8WXH4)
Organism: Homo sapiens (Human)
Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:24337577}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Cullin-5
Sequence:
MEDGPVFYGFKNIFITMFATFFFFKLLIKVFLALLTHFYIVKGNRKEAARIAEEIYGGISDCWADRSPLHEAAAQGRLLALKTLIAQGVNVNLVTINRVSSLHEACLGGHVACAKALLENGAHVNGVTVHGATPLFNACCSGSAACVNVLLEFGAKAQLEVHLASPIHEAVKRGHRECMEILLANNVNIDHEVPQLGTPLYVACTYQRVDCVKKLLELGASVDHGQWLDTPLHAAARQSNVEVIHLLTDYGANLKRRNAQGKSALDLAAPKSSVEQALLLREGPPALSQLCRLCVRKCLGRACHQAIHKLHLPEPLERFLLYQ
Protein: Protein LST8 homolog (Q9W328)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of TORC1 and TORC2, which regulate cell growth and survival in response to nutrient and hormonal signals. Essential for TORC2-mediated regulation of cell growth and phosphorylation of Akt1. However it is not required for TORC1-mediated functions such as TORC1-dependent regulation of cell growth, autophagy and phosphorylation of S6K.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Stress-activated map kinase-interacting protein 1
- Serine/threonine-protein kinase mTor
- Raptor, isoform B
- FI03615p
- LOBE
- GTP-binding protein Rheb homolog
- GH04846p
- LD07294p
- Ribosomal protein S6 kinase
- GH16429p
Sequence:
MGDQQQLILATGGYDHTIKVWQAHTGNCIKTMRFVETSQVNALDRTPDKTRLAACGYQCIRLYDLESNCTAPVINFDGVQKNVTRLGFQEDGNWMFTAGEDHHVRIWDMIAAPPHCSRIFDCEAPVNAACLHPNQVEIAMGSQNGSVFLWDVKSERHERIVPEVDASIQDVAISPDGRYLAAANNKGNCYIWSLTSQDQKMSTLRPNRKIPAHSRYILRCKFSPDSRLLLTTSGDGTVCIWKTDDFSKWRELCIENYWVWDAAFSADSKWLFTASSDGIARLWKLQTKSSIRDYTGHTKAITALSFKDEIVGK
Protein: HL08057p (IP03491p) (Photoreceptor dehydrogenase, isoform A (EC 1.1.1.-, EC 1.1.1.105)) (Q9VV42)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Phosrestin-1
- Guanine nucleotide-binding protein subunit beta-2
- Inactivation-no-after-potential D protein
- Opsin Rh1
- Calphotin
Sequence:
MKPQGIPPTTTRISQTKMSFRGKNAVVTGGAGGIGLQVSKQLLAAGAAKVAIIDLQDNLEEFVKLRAAHPTQSVMIIKMDVANKKGVEATYEEIAKTFGNIDIVVNVAGIFNDKDVQRTLLVNLGGIINSTLSALPYMGKDNGGKGGIVVNMSSVVGLDPMFIIPVYGATKAGIINFTRCLANEKYYQRSGIKFVTVCPGATMTDMFTNFTEKIIFPETSDETYRILDRLNKQSAADVSRCILNVLEKDKNGAVYVIEGKRVYPLEIKPQWTGKEQAL
Protein: At5g10460 (Haloacid dehalogenase-like hydrolase (HAD) superfamily protein) (Q6DBI9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFCSSQLSQPMNGLKDIVETRNFKAWLLDQYGVLHDGKKPYPGAISTLKNLATAGAKIVIISNSSRRASTTMEKLKGLGFDPSFFTGAITSGELTHQSLQRRDDPWFAALGRRCIHITWNDRGAISLEGLDLNVVENVEEADFVLAHGTEALGLPSGSVSPRTIDELEKILEKSAARGLPMIVANPDYVTVEANVFHIMPGTLASKYEELGGEVKSMGKPHKMIYESAIAIAGVNPSESIAVGDSLHHDIRGANVSGIESIFITGGIHGNELGLTSFDETASLDSVKTLTAKHNAFPTYVLSAFKW
Protein: C5a anaphylatoxin chemotactic receptor 2 (Complement component 5a receptor 2) (G-protein coupled receptor 77) (Q9P296)
Organism: Homo sapiens (Human)
Function: Receptor for the chemotactic and inflammatory C3a, C4a and C5a anaphylatoxin peptides and also for their dearginated forms ASP/C3adesArg, C4adesArg and C5adesArg respectively. Couples weakly to G(i)-mediated signaling pathways.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19615750}; Multi-pass membrane protein {ECO:0000269|PubMed:19615750}.
Interaction partners:
- Complement C3
- Complement C5
- Complement C4-A
- C5a anaphylatoxin chemotactic receptor 1
Sequence:
MGNDSVSYEYGDYSDLSDRPVDCLDGACLAIDPLRVAPLPLYAAIFLVGVPGNAMVAWVAGKVARRRVGATWLLHLAVADLLCCLSLPILAVPIARGGHWPYGAVGCRALPSIILLTMYASVLLLAALSADLCFLALGPAWWSTVQRACGVQVACGAAWTLALLLTVPSAIYRRLHQEHFPARLQCVVDYGGSSSTENAVTAIRFLFGFLGPLVAVASCHSALLCWAARRCRPLGTAIVVGFFVCWAPYHLLGLVLTVAAPNSALLARALRAEPLIVGLALAHSCLNPMLFLYFGRAQLRRSLPAACHWALRESQGQDESVDSKKSTSHDLVSEMEV
Protein: Cysteine-rich secretory protein LCCL domain-containing 2 (Coffeecrisp) (Q8BZQ2)
Organism: Mus musculus (Mouse)
Function: Promotes matrix assembly.
Subcellular location: Secreted {ECO:0000269|PubMed:18757743}.
Interaction partners:
Sequence:
MSCLLNNMVLMGLALLVCGVQAFFLPNTTSLEKLLSKYQHAEPHSRVRRAIPMSDRQEILMLHNKLRGQVYPPASNMEHMTWDEELERSAAAWAHRCLWEHGPAGLLRSIGQNLAVHWGRYRSPGFHVQSWYDEVKDYTYPYPHECTPRCRERCSGPMCTHYTQMVWATTNKIGCAVHTCRNMNVWGDTWENAVYLVCNYSPKGNWIGEAPYKHGRPCSECPSSYGGGCLNNLCHRAEKPHKHKPEVDMMNEVESPPAPEETHVWVQPRVIKTKKTPVINFMTQVVHCDTKMKDSCKGSTCNRYQCPAGCLSNKAKVFGSLFYESSSSICRAAIHYGVIDDRGGLVDVTRNGMVPFFVKSQKNGMESLSKYKPSSSFTVSKVTETAVDCHATVAQLCPFEKPATHCPRIQCPARCGEEPSYWAPVYGTNIYADTSSICKAAVHAGVIVDEVGGYADVMPVDKKKSYVGSLRNGVQSESLNTPQNGNAFRIFAVRQ
Protein: AP-3 complex subunit delta (Adaptor-related protein complex 3 subunit delta) (Delta-adaptin) (At-d-Ad) (At-delta-Ad) (Protein-affected trafficking 4) (Q9C744)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of the AP-3 complex, an adaptor-related complex which seems to be clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. It also function in maintaining the identity of lytic vacuoles and in regulating the transition between storage and lytic vacuoles.
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Also localizes to a novel cellular compartment, the 'delta compartment', characterized by colocalization of EPSIN2 and DELTA-ADR. {ECO:0000269|PubMed:17277094}.
Interaction partners:
- AP-3 complex subunit mu
- AP3-complex subunit beta-A
- AP-3 complex subunit sigma
- Electron transporter
- DUF547 domain-containing protein
- DUF547 domain-containing protein
- At1g76620/F14G6_22
- Protein FAR-RED ELONGATED HYPOCOTYL 1
- AP-2 complex subunit sigma
- Vacuolar protein sorting-associated protein 41 homolog
Sequence:
MSSSSTSIMDNLFQRSLEDLIKGFRLQLLGESNFISRAVEEIRREIKATDLSTKSTALHKLSYLAALHGVDMSWAAFHAVEVVSSSRFQHKRIGYQAITQSFNDQTSVMLLITNQVRKDLNSANEYEVSLALECLSRIGTHDLARDLTPEVFTLLGSSKSFVKKKAIGVVLRVFEKYHDAVKVCFKRLVENLETSDPQILSAVVGVFCELATKDPQSCLPLAPEFYKVLVDSRNNWVLIKVLKIFAKLALIEPRLGKKVAEPICEHMRRTVAKSLVFECVRTVVSSLSDNEAAVKLAVAKIREFLVEDDPNLKYLGLNALSIVAPKHLWAVLENKEVVVKAMSDEDPNVKLEALHLLMAMVNEDNVSEISRILMNYALKSDPLFCNEIIFSVLSACSRNAYEIIVDFDWYLSLLGEMARIPHCQRGEDIEHQLIDIGMRVRDARPQLVRVSWALLIDPALLGNLFLHPILSAAAWVSGEYVEFSKNPYETVEALLQPRTDLLPPSIKAIYIHSAFKVLVFCLGSYFSSQEPTSSSLAQESSSGSLLVNVFTHESILSLVNVIELGLGPLSGYHDVEVQERAKNVLGYISVIKQEIAEQLNLQDNETEASRVTAFMEDVFSEEFGPISATAQEKVCVPDGLELKENLGDLEEICGEHLKPVESDSVSYTDKISFSVSKLRIRDQQEATSSSSPPHEASSLLAEHRKRHGMYYLTSQKEDQDSNGTSSDYPLANELANEISQDSFNPKRKPNQSKPRPVVVKLDDGDESRITPQAKTNIQTANDDESLSRAIQSALLVKNKGKEKDRYEGNPNSGQQEKEESSRIENHQNSEKKKKKKKKKKGEGSSKHKSRRQNEVASASEQVIIPDFLL
Protein: Regulatory protein E2 (P03120)
Organism: Human papillomavirus type 16
Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:18619639, ECO:0000269|PubMed:25340539, ECO:0000269|PubMed:25911730, ECO:0000269|PubMed:7645246}.
Interaction partners:
Sequence:
METLCQRLNVCQDKILTHYENDSTDLRDHIDYWKHMRLECAIYYKAREMGFKHINHQVVPTLAVSKNKALQAIELQLTLETIYNSQYSNEKWTLQDVSLEVYLTAPTGCIKKHGYTVEVQFDGDICNTMHYTNWTHIYICEEASVTVVEGQVDYYGLYYVHEGIRTYFVQFKDDAEKYSKNKVWEVHAGGQVILCPTSVFSSNEVSSPEIIRQHLANHPAATHTKAVALGTEETQTTIQRPRSEPDTGNPCHTTKLLHRDSVDSAPILTAFNSSHKGRINCNSNTTPIVHLKGDANTLKCLRYRFKKHCTLYTAVSSTWHWTGHNVKHKSAIVTLTYDSEWQRDQFLSQVKIPKTITVSTGFMSI
Protein: Formyl peptide receptor 2 (Formylpeptide receptor-related sequence 2) (Lipoxin A4 receptor-like protein) (N-formylpeptide receptor-like 2) (O88536)
Organism: Mus musculus (Mouse)
Function: High affinity receptor for N-formyl-methionyl peptides (FMLP), which are powerful neutrophil chemotactic factors. Stimulates chemotaxis in immune cells to site of infection or tissue damage upon recognition of several ligands, such as FMLP, or ligand involved in cell damage, disease or inflammation. Receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-induced osteoclast differentiation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P25090}; Multi-pass membrane protein {ECO:0000305}. Note=Associates with Amyloid-beta protein 42, product of APP, at the cell surface and the complex is then rapidly internalized. {ECO:0000250|UniProtKB:P25090}.
Interaction partners:
- Annexin A1
- fMet-Leu-Phe receptor
- Amyloid-beta precursor protein
- Cathelicidin antimicrobial peptide
- Interleukin-1 beta
- Heme-binding protein 1
- Kallikrein 1-related peptidase b1
Sequence:
MESNYSIHLNGSEVVVYDSTISRVLWILSMVVVSITFFLGVLGNGLVIWVAGFRMPHTVTTIWYLNLALADFSFTATLPFLLVEMAMKEKWPFGWFLCKLVHIVVDVNLFGSVFLIALIALDRCICVLHPVWAQNHRTVSLARKVVVGPWIFALILTLPIFIFLTTVRIPGGDVYCTFNFGSWAQTDEEKLNTAITFVTTRGIIRFLIGFSMPMSIVAVCYGLIAVKINRRNLVNSSRPLRVLTAVVASFFICWFPFQLVALLGTVWFKETLLSGSYKILDMFVNPTSSLAYFNSCLNPMLYVFMGQDFRERFIHSLPYSLERALSEDSGQTSDSSTSSTSPPADIELKAP
Protein: Tachykinin-like peptide-XIII (P.nigriventer tachykinin peptides XIII) (PnTkP-XIII) (U29-ctenitoxin-Pn1m) (U29-CNTX-Pn1m) (P86310)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKDRFYGLM
Protein: Sodium channel protein type 4 subunit alpha (Mu-1) (SkM1) (Sodium channel protein skeletal muscle subunit alpha) (Sodium channel protein type IV subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.4) (P15390)
Organism: Rattus norvegicus (Rat)
Function: Pore-forming subunit of a voltage-gated sodium channel complex through which Na(+) ions pass in accordance with their electrochemical gradient. Alternates between resting, activated and inactivated states. Required for normal muscle fiber excitability, normal muscle contraction and relaxation cycles, and constant muscle strength in the presence of fluctuating K(+) levels (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:16303569, ECO:0000269|PubMed:2559760, ECO:0000269|PubMed:28012039}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35499}.
Interaction partners:
- Sodium channel regulatory subunit beta-1
- Sodium channel regulatory subunit beta-3
- Sodium channel regulatory subunit beta-2
- Sodium channel regulatory subunit beta-4
- Sodium channel protein type 5 subunit alpha
- Sodium channel protein type 2 subunit alpha
- Sodium channel protein type 3 subunit alpha
- Chloride channel protein 1
- Sodium channel protein type 9 subunit alpha
- Calmodulin-1
Sequence:
MASSSLPNLVPPGPHCLRPFTPESLAAIEQRAVEEEARLQRNKQMEIEEPERKPRSDLEAGKNLPLIYGDPPPEVIGIPLEDLDPYYSDKKTFIVLNKGKAIFRFSATPALYLLSPFSIVRRVAIKVLIHALFSMFIMITILTNCVFMTMSNPPSWSKHVEYTFTGIYTFESLIKMLARGFCIDDFTFLRDPWNWLDFSVITMAYVTEFVDLGNISALRTFRVLRALKTITVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALVGLQLFMGNLRQKCVRWPPPMNDTNTTWYGNDTWYSNDTWYGNDTWYINDTWNSQESWAGNSTFDWEAYINDEGNFYFLEGSNDALLCGNSSDAGHCPEGYECIKAGRNPNYGYTSYDTFSWAFLALFRLMTQDYWENLFQLTLRAAGKTYMIFFVVIIFLGSFYLINLILAVVAMAYAEQNEATLAEDQEKEEEFQQMLEKYKKHQEELEKAKAAQALESGEEADGDPTHNKDCNGSLDASGEKGPPRPSCSADSAISDAMEELEEAHQKCPPWWYKCAHKVLIWNCCAPWVKFKHIIYLIVMDPFVDLGITICIVLNTLFMAMEHYPMTEHFDNVLSVGNLVFTGIFTAEMVLKLIAMDPYEYFQQGWNIFDSFIVTLSLVELGLANVQGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKIASDCNLPRWHMNDFFHSFLIVFRILCGEWIETMWDCMEVAGQAMCLTVFLMVMVIGNLVVLNLFLALLLSSFSADSLAASDEDGEMNNLQIAIGRIKWGIGFAKTFLLGLLRGKILSPKEIILSLGEPGGAGENAEESTPEDEKKEPPPEDKELKDNHILNHVGLTDGPRSSIELDHLNFINNPYLTIQVPIASEESDLEMPTEEETDAFSEPEDIKKPLQPLYDGNSSVCSTADYKPPEEDPEEQAEENPEGEQPEECFTEACVKRCPCLYVDISQGRGKMWWTLRRACFKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRRVIRTILEYADKVFTYIFILEMLLKWVAYGFKVYFTNAWCWLDFLIVDVSIISLVANWLGYSELGPIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYYCVNTTTSERFDISVVNNKSESESLMYTGQVRWMNVKVNYDNVGLGYLSLLQVATFKGWMDIMYAAVDSREKEEQPHYEVNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGKDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPQNKIQGMVYDFVTKQVFDISIMILICLNMVTMMVETDDQSQLKVDILYNINMVFIIIFTGECVLKMFALRHYYFTIGWNIFDFVVVILSIVGLALSDLIQKYFVSPTLFRVIRLARIGRVLRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMSNFAYVKKESGIDDMFNFETFGNSIICLFEITTSAGWDGLLNPILNSGPPDCDPTLENPGTNVRGDCGNPSIGICFFCSYIIISFLIVVNMYIAIILENFNVATEESSEPLSEDDFEMFYETWEKFDPDATQFIDYSRLSDFVDTLQEPLKIAKPNKIKLITLDLPMVPGDKIHCLDILFALTKEVLGDSGEMDALKQTMEEKFMAANPSKVSYEPITTTLKRKQEEVCAIKIQRAYRRHLLQRSVKQASYMYRHSQDGNDDGAPEKEGLLANTMNKMYGHEKEGDGVQSQGEEEKASTEDAGPTVEPEPTSSSDTALTPSPPPLPPSSSPPQGQTVRPGVKESLV
Protein: V-type proton ATPase catalytic subunit A isoform 2 (V-ATPase subunit A 2) (EC 7.1.2.2) (V-ATPase 69 kDa subunit 2) (Vacuolar proton pump subunit alpha 2) (Q27331)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit E
- V-type proton ATPase subunit a
- V-type proton ATPase subunit H
- V-type proton ATPase subunit D 1
- V-type proton ATPase subunit C
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit G
Sequence:
MSNLKRFDDEERESKYGRVFAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLKDINELTESIYIPKGVNVPSLSRVASWEFNPLNVKVGSHITGGDLYGLVHENTLVKHKMIVNPRAKGTVRYIAPSGNYKVDDVVLETEFDGEITKHTMLQVWPVRQPRPVTEKLPANHPLLTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELSVEIDGVTESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDDFYDKNFPEFVPLRTKVKEILQEEEDLSEIVQLVGKASLAETDKITLEVAKLLKDDFLQQNSYSSYDRFCPFYKTVGMLRNIIDFYDMARHSVESTAQSENKITWNVIREAMGNIMYQLSSMKFKDPVKDGEAKIKADFEQLHEDLQQAFRNLED
Protein: Chaperonin 60 subunit beta 3, chloroplastic (CPN-60 beta 3) (C0Z361)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in protein assisted folding.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- 20 kDa chaperonin, chloroplastic
- 10 kDa chaperonin 1
- 10 kDa chaperonin 2, chloroplastic
- Heat shock 70 kDa protein 9, mitochondrial
- Heat shock 70 kDa protein 10, mitochondrial
- Heat shock 70 kDa protein 6, chloroplastic
- Protein groES
- Heat shock 70 kDa protein 4
- T-complex protein 1 subunit theta
- 10 kDa chaperonin, mitochondrial
Sequence:
MASTFSATSSMGSSLAPPSNRLSSFVSISSSSFGRTQSIAQRKARFPKIYAAKQLHFNKDGTAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAASKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVLITRGIEKTTKALVAELKKMSKEVEDSELADVAAVSAGNNYEVGNMIAEAMAKVGRKGVVTLEEGKSAENSLYVVEGMQFDRGYISPYFVTDSEKMCAEYENCKLFLVDKKITNARDIISILEDAIKGGYPLLIIAEDIEQEPLATLVVNKLRGTIKVAALKAPGFGERKSQYLDDIAALTGATVIREEVGLQLEKVGPEVLGNAGKVVLTKDTTTIVGDGSTEEVVKKRVEQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKETLANDEEKVGADIVKKALSYPLKLIAKNAGVNGSVVSEKVLSSDNPKHGYNAATGKYEDLMAAGIIDPTKVVRCCLEHASSVAKTFLMSDCVVVEIKEPESAAPAGNPMDNSGYGF
Protein: RNA-binding protein Raly (Maternally-expressed hnRNP C-related protein) (hnRNP associated with lethal yellow protein) (Q64012)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that acts as a transcriptional cofactor for cholesterol biosynthetic genes in the liver. Binds the lipid-responsive non-coding RNA LeXis and is required for LeXis-mediated effect on cholesterogenesis. May be a heterogeneous nuclear ribonucleoprotein (hnRNP) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:27251289}.
Interaction partners:
- CUGBP Elav-like family member 1
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Heterogeneous nuclear ribonucleoprotein M
- Eukaryotic translation initiation factor 2 subunit 2
Sequence:
MSLKIQTSNVTNKNDPKSINSRVFIGNLNTAVVKKSDVETIFSKYGRVAGCSVHKGYAFVQYANERHARAAVLGENGRVLAGQTLDINMAGEPKPNRPKGLKRAATAIYSGYSFDYDYYQDYFCARLFDYRGRLSPVPVPRAVPVKRPRVTVPLVRRVKTTIPVKLFARSTAVTTGSAKIKLKSSELQTIKTELTQIKSNIDALLGRLEQIAEEQKANPDGKKKGDSSSGGGGGSSGGGGSSNVGGGSSGGSGSCSSSSRLPAPQEDTASEAGTPQGEVQTRDDGDEEGLLTHSEEELEHSQDTDAEDGALQ
Protein: Protein alan shepard (Q8MSV2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has a role in the perception of gravity.
Interaction partners:
- Modifier of mdg4
- Centrosome-associated zinc finger protein Cp190
- Zinc finger protein su
Sequence:
MHPRYSPAPPPQQQQQMGGPPHQQQGGGGGGGVSMRGPSNAQQLPPQIPRSQNYSNGSSSSAAAAPLTSRSAFPGAPLTASAVALKGALPQRPPAMTSPAAAAAGAALAAGAPYRGAASWTPQGYAPAAAAAAAAVAQQAAYRYTAPLPQPAYAAYTPHTATTPATTTVSFLSQPVDYYWYGQRVPTAASPSNTNSSSSSNTGSQSGTLSTSLSNTTNTNTNMGPNGTVQNQNQQGGEQLSKTNLYIRGLQQGTTDKDLVNMCAQYGTIISTKAILDKTTNKCKGYGFVDFEQPAFAECAVKGLQGKGVQAQMAKQQEQDPTNLYIANLPPHFKETDLEAMLSKYGQVVSTRILRDQQMNSKGVGFARMESREKCEQIIQMFNGNTIPGAKDPLLVKFADGGPKKKNLFKTPDPNARAWRDVSAEGIPVAYDPTMQQNGVSVNVGTPIGVPYSRFSAPQVGGYPVAGSQWIPGYMMTQVDDQTSYSPQYMQMAAAPPLGVTSYKPEAVNQVQPRGISMMVSGDTGVPYGTMMPQLATLQIGNSYISPTYPYYAPPPTIIPTMPMTDSEQASTAASPDEAYTQYPHQAAPK
Protein: V-type proton ATPase catalytic subunit A isoform 1 (V-ATPase subunit A 1) (EC 7.1.2.2) (V-ATPase 69 kDa subunit 1) (Vacuolar proton pump subunit alpha 1) (P48602)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Interaction partners:
- V-type proton ATPase subunit E
- V-type proton ATPase subunit B
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit H
- V-type proton ATPase subunit D 1
- V-type proton ATPase subunit G
- V-type proton ATPase subunit a
- V-type proton ATPase subunit C
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MSNLRKFKDEERESEYGRVYAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLRDIGVMTNSIYIPKGVNTTALSRSEMWEFNPLNVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYIAPAGNYNLEDIVLETEFDGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTCEIDGVTESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDEYYDKNYPEFVPLRTKVKEILQEEEDLSEIVQLVGKASLAETDKVTLEVAKLLKDDFLQQNSYSPYDRVCPFYKTVGMLRNIMAFYETARHAVESTAQSDNKITWNTIRESMGGIMYQLSSMKFKDPVKDGEQKIKADYDQLYEDLQQAFRNLED
Protein: Transportin2-like protein (Q38AK1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- GTP-binding nuclear protein
- RNA binding protein, putative
Sequence:
MSFAGGYSITSGDVVKVLHLLRDNGVNVHNSKKAYEELQRYQSDSTFFVLLSYLFGAETCPVDVDLGGNWVQYRRLAGITLKNNLERCKLALGEAAIREAAGCSLAVLVNPTDVRIARVAAQIVVKITVLTSFSWWEECGLGNLPNTLLNDLLMAGEVKTFSALYTLQYLVEDLPEEVGLASKDIIERVAVLVLDPNAQWGVRKAAFRMCSNMYEQAQSLDWNVESLSPLQIGLTSGSRTFTNLCCLLSEQNCGGDVELKIQVFRSCGVMLDYLEYFTPMPESDMARFIKCWSRDTICTSVSAGIVTEHDVQLKISAIDLLTLTMEMYDKMGGEGYICALIQPLIESLPSLVSALVTYVPMTREDVENILSEDDCSMRDPAAVDFHLNEQKYDISEDSALDDNHGTATLRSTALRCIDALCVLSSKQTFPHLIEKVKALWDGEWQYKEAAIVLVGAMANGCYDEIGDTLPAVVEQLISAVLSPSENIFVVSMSLWSLSRVLEWTYAQDDSTISKIINAFASRLQSRSKRVRHAAVTAINTAFMTAHTMGTTEKVTGDLPSLIEMVISCLPFYNDGNLFILCDLAMHLAALSEDQNTVALLSAAFRANRIERTKGFETTYVAYYINETPNVFVDKDVFSVDRAIIGMLTRFPDPAVSLELLDAWSVVLRDIIERNIRDDISLLLNVLFIAANCANVTPSSSLAGWCSRTQGCIAVLAFQLFNPSEELAVQVAAVTLLHRLLKNAGTCAFPQGIVEELLGKLTSSVITAGDLQNKLEFVYLIMLMVKSYSHESPNGVFCAFKAAVDVLRSDAFSESQLLFSQMAFEVCSALEAAPGLVVHARPDVITRIITECENAYDKSVATIHLVNVLLAVEDVARDILPDVMRLVYSWRQSACNFPGTHESIKLLLSFYSNKHSSLLREQLGLVDSNIREMVISSYGLIC