wanglab/gogpt-training-data huggingface dataset:
Protein: Prolactin receptor (PRL-R) (Q08501)
Organism: Mus musculus (Mouse)
Function: This is a receptor for the anterior pituitary hormone prolactin.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Prolactin
- Prolactin-6A1
- Prolactin-5A1
- Tyrosine-protein kinase JAK2
- Cytokine-inducible SH2-containing protein
- Somatotropin
- Signal transducer and activator of transcription
- Tyrosine-protein kinase JAK3
- Leptin
- Interleukin-7
Sequence:
MSSALAYMLLVLSISLLNGQSPPGKPEIHKCRSPDKETFTCWWNPGSDGGLPTNYSLTYSKEGEKNTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNEMGSSTSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWLPPTITDVKTGWFTMEYEIRLKSEEADEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWGQEKSIEIPNDFTLKDTTVWIIVAVLSAVICLIMVWAVALKGYSMMTCIFPPVPGPKIKGFDTHLLEKGKSEELLSALGCQDFPPTSDCEDLLVEFLEVDDNEDERLMPSHSKEYPGQGVKPTHLDPDSDSGHGSYDSHSLLSEKCEEPQAYPPAFHIPEITEKPENPEANIPPTPNPQNNTPNCHTDTSKSTTWPLPPGQHTRRSPYHSIADVCKLAGSPGDTLDSFLDKAEENVLKLSEDAGEEEVAVQEGAKSFPSDKQNTSWPPLQEKGPIVYAKPPDYVEIHKVNKDGVLSLLPKQRENHQTENPGVPETSKEYAKVSGVTDNNILVLVPDSRAQNTALLEESAKKVPPSLEQNQSEKDLASFTATSSNCRLQLGRLDYLDPTCFMHSFH
Protein: Angiopoietin-related protein 7 (Angiopoietin-like factor) (Angiopoietin-like protein 7) (Cornea-derived transcript 6 protein) (O43827)
Organism: Homo sapiens (Human)
Function: Has a role in the formation and organization of the extracellular matrix. In the eye, it functions as a mediator of dexamethasone-induced matrix deposition in the trabecular meshwork, the tissue responsible for the outflow of the ocular aqueous humor and for the maintenance of intraocular pressure. Is a negative regulator of angiogenesis in the cornea, and plays a major role in maintaining corneal avascularity and transparency.
Subcellular location: Secreted {ECO:0000269|PubMed:11682471}.
Interaction partners:
Sequence:
MLKKPLSAVTWLCIFIVAFVSHPAWLQKLSKHKTPAQPQLKAANCCEEVKELKAQVANLSSLLSELNKKQERDWVSVVMQVMELESNSKRMESRLTDAESKYSEMNNQIDIMQLQAAQTVTQTSADAIYDCSSLYQKNYRISGVYKLPPDDFLGSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEHIHRLSRQPTRLRVEMEDWEGNLRYAEYSHFVLGNELNSYRLFLGNYTGNVGNDALQYHNNTAFSTKDKDNDNCLDKCAQLRKGGYWYNCCTDSNLNGVYYRLGEHNKHLDGITWYGWHGSTYSLKRVEMKIRPEDFKP
Protein: Probable cation-transporting ATPase C1672.11c (EC 7.2.2.-) (O74431)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Cation-transporting ATPase 5
Sequence:
MASPKMIRSKRSTSSIASKNSLNSYLASSLMSHDSIFDGPGLGTSIPSSVSSFHHQTLRPSSDASVSQFSMDYLQSEYNLNRYNDGESIAASRDYQSLLRDNGSGVYSDEEEITEMMLEELNIHPVLRRESVGEAAGLSEDGCCQILYLVEEDLEVGIAGYKTNKSRYRLYQAICLLTLGLAYLIFRWLPKYFIRFVGTREPLATADWLTIETQWGELSKLDIQIQPYENSLSSIFGASIRVAAPEGTENDPFIENFRYVNYRYMKLIFHPLLDRFLIQQDWKDPRWIRDTSVVKEGLERDAINDRLCIFGENLIDLELKSVSQLLIDEVLHPFYIFQVFSIILWSMDSYYYYAICILIISVVSILGSLIETRKTLRRMREMSRFTCPVRVYRDGFWTSISSTDLVIGDVFEISDPELTIFPADALLLSGDCIVNESMLTGESIPVSKIPATDQSMKELFSFSKNIPASLCKHFLFSGTKIIQVRKPFVNEKEEGASLAMVVRTGFNTTKGALVRSMIFPKPTNFSFYRDSFRFITAMFIIALIGFVFSSINLLTLGVPIATIIIRALDLITIVVPPALPATLTIGTTFAISRLRKQGIFCISPQRVNVSGKLDLISFDKTGTLTEDGLDIMGVSVIEGSELGDLRSNSGNLCSKDLLSNDSPSNLLYTMATCHMLRYVDGELVGDPLDIKMFKFTHWSYSEENFLNKKMSSEQAEDAAYVRTQQLIPPTVSPPWNSPSNNYTESDLELGIVRTFEFVSQLRRMAVIVKHGKFKKMDAYVKGAPEIMPSICKPESFPANYQEVLDYYTHNGFRVIACASKQLENCTWAKAQRMKREQVECDLDFCGFIVFENKLKSTTATVIRELNDARIRTVMCTGDNVLTSICVGKRCGMLPEDGYVFLPRFDEESESADEASRQLVWQAIENNEIFLDPHTLRPNVDFADHEPVSIELARLKDFHIALTGDVFRWLVDYAPLNVFHHILLKAQIFARMSPSEKNELVSCFQNLNYCVGFCGDGANDCGALKAADVGISLSEAEASVAAPFTSKWFEITCVLDVIKDGRAALVTSFSCFQYMALYSAIQFITVSILYTTNSNLGDFQFLFIDLVIILPIAVFMGRSRPYHRLAHKRPTANLVSKRILSPLIGQIVLICIIQYITLRIVRREPWYIPPPANSSDTNITNSDVTALFLISCFQYIFIGVVLSIGPPYREKVWRNYSFTAVVVVLLILTVKLIRLQNHKNFFMKLFQLTPTSKSFQNFLIFAGVIYYLLAASGQNYIFISMTNFISHLNNRLLNRRTKVSKKLYKRLFADLQNEQV
Protein: Cytokinin dehydrogenase 7 (EC 1.5.99.12) (Cytokinin oxidase 7) (AtCKX5) (AtCKX7) (CKO7) (Q9FUJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. Catalyzes in vitro the oxidation of various types of cytokinin nucleotides that are known as direct products of cytokinin biosynthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24528491}.
Interaction partners:
- Adenylate isopentenyltransferase 5, chloroplastic
- tRNA dimethylallyltransferase 2
- Histidine kinase 4
- Adenylate isopentenyltransferase 3, chloroplastic
- tRNA dimethylallyltransferase 9
- Adenylate isopentenyltransferase 1, chloroplastic
- Histidine kinase 3
- Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG1
- Adenylate isopentenyltransferase 7, mitochondrial
- Cytokinin hydroxylase
Sequence:
MIAYIEPYFLENDAEAASAATAAGKSTDGVSESLNIQGEILCGGAAADIAGRDFGGMNCVKPLAVVRPVGPEDIAGAVKAALRSDKLTVAARGNGHSINGQAMAEGGLVVDMSTTAENHFEVGYLSGGDATAFVDVSGGALWEDVLKRCVSEYGLAPRSWTDYLGLTVGGTLSNAGVSGQAFRYGPQTSNVTELDVVTGNGDVVTCSEIENSELFFSVLGGLGQFGIITRARVLLQPAPDMVRWIRVVYTEFDEFTQDAEWLVSQKNESSFDYVEGFVFVNGADPVNGWPTVPLHPDHEFDPTRLPQSCGSVLYCLELGLHYRDSDSNSTIDKRVERLIGRLRFNEGLRFEVDLPYVDFLLRVKRSEEIAKENGTWETPHPWLNLFVSKRDIGDFNRTVFKELVKNGVNGPMLVYPLLRSRWDDRTSVVIPEEGEIFYIVALLRFVPPCAKVSSVEKMVAQNQEIVHWCVKNGIDYKLYLPHYKSQEEWIRHFGNRWSRFVDRKAMFDPMAILSPGQKIFNRSL
Protein: Argininosuccinate lyase (ASAL) (EC 4.3.2.1) (Arginosuccinase) (P04424)
Organism: Homo sapiens (Human)
Function: Catalyzes the reversible cleavage of L-argininosuccinate to fumarate and L-arginine, an intermediate step reaction in the urea cycle mostly providing for hepatic nitrogen detoxification into excretable urea as well as de novo L-arginine synthesis in nonhepatic tissues. Essential regulator of intracellular and extracellular L-arginine pools. As part of citrulline-nitric oxide cycle, forms tissue-specific multiprotein complexes with argininosuccinate synthase ASS1, transport protein SLC7A1 and nitric oxide synthase NOS1, NOS2 or NOS3, allowing for cell-autonomous L-arginine synthesis while channeling extracellular L-arginine to nitric oxide synthesis pathway.
Interaction partners:
- Argininosuccinate synthase
- N-acetylglutamate synthase, mitochondrial
- Ornithine aminotransferase, mitochondrial
- Arginase-2, mitochondrial
- Arginase-1
- Nitric oxide synthase 3
- Ornithine transcarbamylase, mitochondrial
- Adenylosuccinate lyase
- Nitric oxide synthase 1
- Nitric oxide synthase, inducible
Sequence:
MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA
Protein: RING finger protein 24 (Q9Y225)
Organism: Homo sapiens (Human)
Function: May play a role in TRPCs intracellular trafficking.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17850865}; Single-pass membrane protein {ECO:0000269|PubMed:17850865}.
Interaction partners:
- Short transient receptor potential channel 6
Sequence:
MSSDFPHYNFRMPNIGFQNLPLNIYIVVFGTAIFVFILSLLFCCYLIRLRHQAHKEFYAYKQVILKEKVKELNLHELCAVCLEDFKPRDELGICPCKHAFHRKCLIKWLEVRKVCPLCNMPVLQLAQLHSKQDRGPPQGPLPGAENIV
Protein: Beta-theraphotoxin-Ps1a (Beta-TRTX-Ps1a) (PaurTx-III) (Phrixotoxin-3) (PaurTx3) (P84510)
Organism: Paraphysa scrofa (Chilean copper tarantula) (Phrixotrichus auratus)
Function: Potent inhibitor of Nav1.2/SCN2A voltage-gated sodium channels (IC(50)=0.6-0.7 nM). Also weakly inhibits Nav1.1/SCN1A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.7/SCN9A and Nav1.8/SCN10A (IC(50)=20-610 nM). It acts by shifting the voltage dependence of channel activation to more depolarized potentials and by blocking the inward component of the sodium current. It shows low affinity for lipid bilayers. In vivo, this toxin causes general ataxia, lack of response to stimuli, and semiparalysis. After a few minutes, the mice are unable to stand, and breathing is reduced in rhythm and intensity. Symptoms gradually increase with progressive slowing of breathing and flaccid paralysis; death occurred within 10 to 20 minutes post injection. Animals remain totally flaccid, and no symptoms of excitatory neurotoxicity are observed.
Subcellular location: Secreted {ECO:0000269|PubMed:16267209}.
Interaction partners:
Sequence:
DCLGFLWKCNPSNDKCCRPNLVCSRKDKWCKYQI
Protein: Voltage-dependent calcium channel gamma-1 subunit (Dihydropyridine-sensitive L-type, skeletal muscle calcium channel subunit gamma) (P19518)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics.
Subcellular location: Cell membrane, sarcolemma {ECO:0000269|PubMed:12409298, ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036, ECO:0000305|PubMed:2158672}; Multi-pass membrane protein {ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036}.
Interaction partners:
Sequence:
MSPTEAPKVRVTLFCILVGIVLAMTAVVSDHWAVLSPHMENHNTTCEAAHFGLWRICTKRIALGEDRSCGPITLPGEKNCSYFRHFNPGESSEIFEFTTQKEYSISAAAISVFSLGFLIMGTICALMAFRKKRDYLLRPASMFYVFAGLCLFVSLEVMRQSVKRMIDSEDTVWIEYYYSWSFACACAAFVLLFLGGISLLLFSLPRMPQNPWESCMDAEPEH
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Alpha-D-glucosyl-1-phosphate uridylyltransferase) (UDP-Glc PPase) (UDP-glucose pyrophosphorylase) (UDPGP) (Uridine diphosphoglucose pyrophosphorylase) (P0AEP3)
Organism: Escherichia coli (strain K12)
Function: May play a role in stationary phase survival.
Interaction partners:
- UDP-glucose 4-epimerase
- Phosphoglucomutase
- UDP-glucose 6-dehydrogenase
- Galactokinase
- Type IV methyl-directed restriction enzyme EcoKMrr
- Type IV methyl-directed restriction enzyme EcoKMcrA
- Galactose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Glucose-1-phosphate adenylyltransferase
- Trehalose-6-phosphate synthase
Sequence:
MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMVEPVADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK
Protein: Nuclear receptor subfamily 4 group A member 2 (A0A2R9YJF7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MPCVQAQYGSSPQGASPASQSYSYHTSGEYSCDFLTPEFVKFSMDLTNTEITAATTSLPSFSTFMDNYNTSYDVKPPCLYQVPHSGEQSSIKVEDVQMHTYHQQSHLGPQSEEMMAHPGPMYFKPSSPHGPGPANFQVQPNHMWEDPGSLHTFHQNYMTSHMIDQRKNPVSRLSLFSFKQSPPGTPVSSCQMRFDGPLHVSMHDSTGAHRTLDSQSFAVPSTIRKQAGIAFTHSLQLSHGHQLMDSQVPSPPSRGSPSTEGLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLVVGMVKEVVRTDNLKGRRGRLPSKPKSPQESSPPSPPVSLISALVRAHVDSNPSMNSLDYTRFQANPDYQLSGDDTQHIQQFYDLLTGSMEIIRGWAEKIPGFTDLPKPDQDLLFESAFLELFVLRLAYRSNPMESKLIFCNGVVLHRLQCVRGFGEWIDSIVEFSSNLQNMNLDISAFSCIAALAMVTERHGLKEPKRVEDLQNKIVNCLKDQVTFNGGGLNRPNYLSKLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPAIIDKLFLDTLPF
Protein: Long chain acyl-CoA synthetase 5 (EC 6.2.1.3) (Q9T009)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Interaction partners:
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Peroxisomal acyl-coenzyme A oxidase 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Acyl-coenzyme A oxidase 2, peroxisomal
- Acyl-coenzyme A oxidase 3, peroxisomal
- Acyl-coenzyme A oxidase 4, peroxisomal
- Putative acyl-coenzyme A oxidase At3g06690
- Putative acyl-coenzyme A oxidase 3.2, peroxisomal
Sequence:
MTSQKRFIFEVEAAKEATDGNPSVGPVYRSTFAQNGFPNPIDGIQSCWDIFRTAVEKYPNNRMLGRREISNGKAGKYVWKTYKEVYDIVIKLGNSLRSCGIKEGEKCGIYGINCCEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHAEVSIAFVEEKKIPELFKTCPNSTKYMKTVVSFGGVKPEQKEEAEKLGLVIHSWDEFLKLGEGKQYELPIKKPSDICTIMYTSGTTGDPKGVMISNESIVTITTGVMHFLGNVNASLSEKDVYISYLPLAHVFDRAIEECIIQVGGSIGFWRGDVKLLIEDLGELKPSIFCAVPRVLDRVYTGLQQKLSGGGFFKKKVFDVAFSYKFGNMKKGQSHVAASPFCDKLVFNKVKQGLGGNVRIILSGAAPLASHIESFLRVVACCNVLQGYGLTESCAGTFATFPDELDMLGTVGPPVPNVDIRLESVPEMNYDALGSTPRGEICIRGKTLFSGYYKREDLTKEVFIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLAQGEYVAVENLENVYSQVEVIESIWVYGNSFESFLVAIANPAQQTLERWAVENGVNGDFNSICQNAKAKAFILGELVKTAKENKLKGFEIIKDVHLEPVAFDMERDLLTPTYKKKRPQLLKYYQNVIHEMYKTTKESLASGQ
Protein: SUMO family protein (Q59W54)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- SUMO protease
- Nucleoporin
- SUMO ligase
- SUMO-conjugating enzyme UBC9
- Ubiquitin-activating enzyme E1-like
- SUMO protease
- Nucleoporin NSP1
- E1 ubiquitin-activating protein
- Proliferating cell nuclear antigen
- GTPase-activating protein
Sequence:
MSDTENTGGSPPAAEAGPKEEKGTHINVKVSDGTQEVFFKVKRNTKFRRLMEAFAKRQGTSPDTMRFLVDGGRVHADQTPEDLDMDDGDTIEAHRAQIGGCL
Protein: Zinc/cadmium/lead-transporting P-type ATPase (EC 7.2.2.-) (EC 7.2.2.12) (EC 7.2.2.21) (Pb(II)/Cd(II)/Zn(II)-translocating ATPase) (Zn(2+)/Cd(2+)/Pb(2+) export ATPase) (P37617)
Organism: Escherichia coli (strain K12)
Function: Confers resistance to zinc, cadmium and lead. Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes. Can also bind nickel, copper, cobalt and mercury.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:10660539, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16411752, ECO:0000269|PubMed:16890908}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- HTH-type transcriptional regulator ZntR
- Zinc transporter ZupT
- Zinc transporter ZitB
- Cation-efflux pump FieF
- Copper-exporting P-type ATPase
- Arsenical resistance operon repressor
- HTH-type transcriptional regulator CueR
- Multicopper oxidase CueO
- Zinc import ATP-binding protein ZnuC
- High-affinity zinc uptake system protein ZnuA
Sequence:
MSTPDNHGKKAPQFAAFKPLTTVQNANDCCCDGACSSTPTLSENVSGTRYSWKVSGMDCAACARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVESALQKAGYSLRDEQAAEEPQASRLKENLPLITLIVMMAISWGLEQFNHPFGQLAFIATTLVGLYPIARQALRLIKSGSYFAIETLMSVAAIGALFIGATAEAAMVLLLFLIGERLEGWAASRARQGVSALMALKPETATRLRKGEREEVAINSLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGDKVPAGATSVDRLVTLEVLSEPGASAIDRILKLIEEAEERRAPIERFIDRFSRIYTPAIMAVALLVTLVPPLLFAASWQEWIYKGLTLLLIGCPCALVISTPAAITSGLAAAARRGALIKGGAALEQLGRVTQVAFDKTGTLTVGKPRVTAIHPATGISESELLTLAAAVEQGATHPLAQAIVREAQVAELAIPTAESQRALVGSGIEAQVNGERVLICAAGKHPADAFTGLINELESAGQTVVLVVRNDDVLGVIALQDTLRADAATAISELNALGVKGVILTGDNPRAAAAIAGELGLEFKAGLLPEDKVKAVTELNQHAPLAMVGDGINDAPAMKAAAIGIAMGSGTDVALETADAALTHNHLRGLVQMIELARATHANIRQNITIALGLKGIFLVTTLLGMTGLWLAVLADTGATVLVTANALRLLRRR
Protein: IQ motif and SEC7 domain-containing protein 1 isoform X3 (IQ motif and Sec7 domain ArfGEF 1b) (X1WBR0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLKLKTFCLDYWQFLCLQPLNGFYKSVEGEAPGGESGPSLDNSGGYLRGPVSRSAIISGEHFDGPPLYAHEVRQRPRRPKLQHSQSILRKQAEEEAIKRSRSLSESYELSTDLQDKQVEMLERKYGGRFITRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSLTDDGSKLGALVQSERGEMVPANMKSPAVQSDFTDAITELEDVFSRQVKSLAESIDDALNCRSLHGDEGQSEATRGHPDLEQEVTYQVKPSHGSEHRKRDEMTASYSDVTLYIDEEELSPPLPLSQSVDRPSSTESDLRLRSLNSSQDYWSLAHKDEKADTDTSCRSTPSLECQEQRLRIDHLPLLTIEPPSDSSVELSDRSDRSSLKRQNAYDRGIASQQGSPKHIPSHALPPRGPAREDEAPRHRPRQLESHLAINGTANRQSKSESDFSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKETRNSWDSPAFSNDIIRKRHYRIGLNLFNKKPEKGIQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSAMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCICNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFVKNLRGVDDGEDIPREMLVGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHHGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGVRLTSALPGADIKVLINFNAPNPQDRKKFTDDLRESIAEVQEMEKYRIESELEKQKGVVRPSISQSSGLKKETGNGNLSRTSLDDSYAMGEGLKRSALSSSLRDLSDAGKRGRRSSAGSLDSNMEGSIISSPHIRRRATSSRDCPSRQQSIPNSSSLLGSLFGTKRGKSPSLPSQSSHPSHPTLISHTPHPSNLHHTARDGVTVTETQAQMHPHHAQFCHMQNPPPYHHHHHYHPPAHIQHPPHQYHPPPGPSSSHSHSHSQHGHGPHPSHSSHPSHSQHAPHHHSQPPAPPPAASSTKPKHSGISTVV
Protein: Entomoglyceroporin 4, isoform E (MIP15905p) (D1Z394)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNLEQQGMDPQGVENQQEIVQAAEGEQQLQSCCKVFKMKGSTLDKISAFLGELIGTGILVFLGCMGCVKTDLFPNNHLQIVLNFGFAVLIAIQCFGCVSGAHLNPAVTVAAYIYEMVTLRMAFAYFAAQMLGAFIGYGLLMVLLPSPTLTVGAGLCVTLPHTSVTTGQALGIEFVITSILVIVCCGVWDPRNSKFHDSVGIRFGLAIACLACAAGPFTGGSMNPARSFAPALWNKHFESNWIYWLAPLSSSAITAYAYKVVFRREVVEAEITSNEKLRQLEDVQLS
Protein: Zinc finger CCCH-type containing, antiviral 1 (C9J6P4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADPEVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVATTRARVCRRKYCQRPCDNLHLCKLNLLGRCNYSQSERNLCKYSHEVLSEENFKVLKNHELSGLNKEELAVLLLQSDPFFMPEICKSYKGEGRQQICNQQPPCSRLHICDHFTRGNCRFPNCLRSHNLMDRKVLAIMREHGLNPDVVQNIQDICNSKHMQKNPPGPRAPSSHRRNMAYRARSKSRDRFFQGSQEFLASASASAERSCTPSPDQISHRASLEDAPVDDLTRKFTYLGSQDRARPPSGSSKATDLGGTSQAGTSQRFLENGSQEDLLHGNPGSTYLASNSTSAPNWKSLTSWTNDQGARRKTVFSPTLPAARSSLGSLQTPEAVTTRKGTGLLSSDYRIINGKSGTQDIQPGPLFNNNADGVATDITSTRSLNYKSTSSGHREISSPRIQDAGPASRDVQATGRIADDADPRVALVNGKYKGKTLWASTFVHDIPNGSSQVVDKTTDVEKTGATGFGLTMAVKAEKDMLRTGSQSLRNLVPTTPGESTAPAQVSTLPQSPAALSSSNRAAVWGAQGQNCTQVPVSSASELTRKTTGSAQYSLSDVTSTTSSRVDDHDSEEICLDHLCKGCPLNGSCSKVHFHLPYRWQMLIGKTWTDFEHMETIEKGYCNPGIHLCSVGSYTINFRVMSCDSFPIRRLSTPSSVTKPANSVFTTKWIWYWKNESGTWIQYGEEKDKRKNSNVDSSYLESLYQSCPRGVVPFQAGSRNYELSFQGMIQTNIASKTQKDVIRRPTFVPQWYVQQMKRGPDHQPAKTSSVSLTATFRPQEDFCFLSSKKYKLSEIHHLHPEYVRVSEHFKASMKNFKIEKIKKIENSELLDKFTWKKSQMKEEGKLLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNCPYDAKNVVMFVAQVLVGKFTEGNITYTSPPPQFDSCVDTRSNPSVFVIFQKDQVYPQYVIEYTEDKACVIS
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 2 (Q0VGB7)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair (By similarity). Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Note=Ionizing radiation induces relocalization to nuclear foci and colocalization with RPA2. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 3A
- Serine/threonine-protein phosphatase 4 regulatory subunit 3B
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Sequence:
MDVERLQEALKDFEKRGKKEVCPVLDQFLCHVAKTGETMIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKIVTGFNGIPFTIQRLCELLTDPRRNYTGTDKFLRGVEKNVMVVSCVCPSSEKNNSNSLNRMNGVMFPGNSPNYTDRSNINGPGTPRPLNRPKLSLSAPLTTNGLPESTDSKDSELQLSEEKGHSDSSASESEVSLLSPVKNKHPDEDAVESEEHEVKRLKFDKEGDVRETASQTVSGEVSSVRAEETETAAPPPDKDRESRTRQHCTEEEEEEEEEEEEEEEESFMTPREMVPERKNQEKESDDALTVNEETSEESHQMEGSGVSPAQTDSTSERSDSAGASRSGSDCLETQESGGPPSSKTGESVSVPSSMESEEATEVTDDPMEQD
Protein: Janus kinase and microtubule-interacting protein 1 (GABA-B receptor-binding protein) (Multiple alpha-helices and RNA-linker protein 1) (Marlin-1) (Q96N16)
Organism: Homo sapiens (Human)
Function: Associates with microtubules and may play a role in the microtubule-dependent transport of the GABA-B receptor. May play a role in JAK1 signaling and regulate microtubule cytoskeleton rearrangements.
Subcellular location: Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Note=Colocalizes with the microtubule network. Localizes to the cell body and neurites of hippocampal neurons where it accumulates in granules. Localizes to the tail and to a lower extent to the head of sperm cells.
Interaction partners:
- Non-receptor tyrosine-protein kinase TYK2
- Gamma-aminobutyric acid type B receptor subunit 2
Sequence:
MSKKGRSKGEKPEMETDAVQMANEELRAKLTSIQIEFQQEKSKVGKLRERLQEAKLEREQEQRRHTAYISELKAKLHEEKTKELQALREGLIRQHEQEAARTAKIKEGELQRLQATLNVLRDGAADKVKTALLTEAREEARRAFDGERLRLQQEILELKAARKQAEEALSNCMQADKTKAADLRAAYQAHQDEVHRIKRECERDIRRLMDEIKGKDRVILALEKELGVQAGQTQKLLLQKEALDEQLVQVKEAERHHSSPKRELPPGIGDMVELMGVQDQHMDERDVRRFQLKIAELNSVIRKLEDRNTLLADERNELLKRSRETEVQLKPLVEKNKRMNKKNEDLLQSIQRMEEKIKNLTRENVEMKEKLSAQASLKRHTSLNDLSLTRDEQEIEFLRLQVLEQQHVIDDLSLERERLLRSKRHRGKSLKPPKKHVVETFFGFDEESVDSETLSETSYNTDRTDRTPATPEEDLDDATAREEADLRFCQLTREYQALQRAYALLQEQVGGTLDAEREARTREQLQADLLRCQAKIEDLEKLLVEKGQDSKWVEEKQLLIRTNQDLLEKIYRLEMEENQLKNEMQDAKDQNELLEFRVLELEVRDSICCKLSNGADILFEPKLKFM
Protein: Tumor necrosis factor receptor superfamily member 5 (B-cell surface antigen CD40) (CD40L receptor) (F6SVZ3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
HLPLPPDDKQYLQGGECCDLCQPGNRLVSHCTALEKTQCQPCDSGEFSAHWNREIRCHQHRHCELNQGLQVKKEGTAVSDTVCTCKEGQHCASKECETCAQHTPCGPGFGVVQMATETTDTVCQPCPVGFFSNGSSLFEKCHPWTSCEDQKLMVLREGTSQTDTLCGFQPRMRALLVIPVVMVILITIFVVFLYIKKVVKKPKDNEVLPPEARGQDPVEIEDYPGHNTAAPVQETLHGCQPVAQEDGKESRISVQERQVTGSMALKPLV
Protein: Serine/arginine-rich-splicing factor 11 (Q5T757)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MINNHRNQALYFSEHKYFQQTQVVYQGDIFWVFLCVFCLRKECVLMQGCFSAGVIPDEAKALSLLAPANAVAGLLPGGGLLPTPNPLTQIGAVPLAALGAPTLDPALAALGLPGANLNSQSLAADQLLKLMSTVDPKLNHVAAGLVSPSLKSDTSSKEIEEAMKRVREAQSLISAAIEPDKKEEKRRHSRSRSRSRRRRTPSSSRHRRSRSRSRRRSHSKSRSRRRSKSPRRRRSHSRERGRRSRSTSKTRDKKKEDKEKKRSKTPPKSYSTARRSRSASRERRRRRSRSGTRSPKKPRSPKRKLSRSPSPRRHKKEKKKDKDKERSRDERERSTSKKKKSKDKEKDRERKSESDKDVKQVTRDYDEEEQGYDSEKEKKEEKKPIETGSPKTKECSVEKGTGDSLRESKVNGDDHHEEDMDMSD