wanglab/gogpt-training-data huggingface dataset:
Protein: Regulator of G-protein signaling 17 (RGS17) (Regulator of Gz-selective protein signaling 2) (Q9QZB0)
Organism: Mus musculus (Mouse)
Function: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Binds selectively to GNAZ and GNAI2 subunits, accelerates their GTPase activity and regulates their signaling activities. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins.
Subcellular location: Membrane {ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. Synapse, synaptosome {ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. Nucleus {ECO:0000269|PubMed:16900103}. Cytoplasm {ECO:0000269|PubMed:16900103}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Regulator of G-protein signaling 7-binding protein
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MRKRQQSQNEGTQAVSQAPGNQRPNNTCCFCWCCCCSCSCLTVRNEERGDSSGRSPHTTKMESIQVLEECQNPTADEVLSWSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKAVEEKARMIYEDYISILSPKEVSLDSRVREVINRSLLDPSPHMYEDAQLQIYTLMHRDSFPRFLNSQIYKAFVESTTSCTSES
Protein: Myeloid-associated differentiation marker-like protein 2 (A6NDP7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGSTMEPPGGAYLHLGAVTSPVGTARVLQLAFGCTTFSLVAHRGGFAGVQGTFCMAAWGFCFAVSALVVACEFTRLHGCLRLSWGNFTAAFAMLATLLCATAAVLYPLYFARRECSPEPAGCAARDFRLAASVFAGLLFLAYAVEVALTRARPGQVSSYMATVSGLLKIVQAFVACIIFGALVHDSRYGRYVATQWCVAVYSLCFLATVAVVALSVMGHTGGLGCPFDRLVVVYTFLAVLLYLSAAVIWPVFCFDPKYGEPKRPPNCARGSCPWDSQLVVAIFTYVNLLLYVVDLAYSQRIRFVPSL
Protein: Splicing factor 3A subunit 2 (SF3a66) (Spliceosome-associated protein 62) (SAP 62) (Q62203)
Organism: Mus musculus (Mouse)
Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3A complex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex. Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes, including the Bact complex. Interacts directly with the duplex formed by U2 snRNA and the intron.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.
Interaction partners:
- Splicing factor 3B subunit 2
- Splicing factor 3B subunit 3
- Splicing factor 3A subunit 1
- Splicing factor 3A subunit 3
- Splicing factor 3B subunit 4
- Splicing factor 3B subunit 1
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 5
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing factor 6
Sequence:
MDFQHRPGGKTGSGGVASSSESNRDRRERLRQLALETIDINKDPYFMKNHLGSYECKLCLTLHNNEGSYLAHTQGKKHQTNLARRAAKEAKEAPAQPAPEQVKVEVKKFVKIGRPGYKVTKQRDTEMGQQSLLFQIDYPEIAEGIMPRHRFMSAYEQRIEPPDRRWQYLLMAAEPYETIAFKVPSREIDKAEGKFFFLQFHFKMEKPPAPPSLPAGPPGVKRPPPPLMNGLPPRPPLPDALPPPPPGGLPLPPMPPTGPAPSGPPGPPQMPPPAPGVHPPAPVVHPPTSGVHPPAPGVHPPAPVVHPPTSGVHPPAPGVHPPTPGVHPPAPGVHPPAPGVHPPAPGVHPPTPGVHPPAPGVHPPAPGVHPPAPGVHPPPSAGVHPQAPGVHPPAPAVHPQAPGVHPPAPGIHPQAPGVHPQPPPGVHPAAPGVHPQPPGVHPSNPGVHPAPMPPMLRPPLPSDGPGNMPPPPPGN
Protein: Protein phosphatase, Mg2+/Mn2+ dependent 1A (E9PJN3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSR
Protein: WASp, isoform C (Q86B74)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRRKLKTLNTAVVQIYKTEGSAHAHWKKRHTGVVCFVKDSAIRSYFMRAYCLIKNELIWEHEIYDGMEVVKSRPFLLTFEGSDGHVGLNFVSEEECDSFFRIVDATIETRNRKRQEKRNRQKSQQAPNAPLPQVQREPARPPPMQGGLSSTDGVQLRNNKINSVTLTPAPAPAQSKNFLSSSFGLGNNAKDKKRKVTKADISRPTNFVHLSHVGWDAQKGFDLAGNENDEVLNEFFVKAGVSEVELKDRDTRAFIYDFIQSNNVLASVKQYSVESPTETAAPMPPPVPTRHPSNGNQRTAPPLPPARQPPPAVPVTVPGAARAPPPPNRPPPISTAPPPPPVSAPVVAPPPPPPPPPAAVPPPPPPPMPVGEIPVITTTHAPTQAARPAAPAAPDPRNALMDAIRKGTQLKKVDTTALSTGSGDSRSDLMKDIRQGTVLKPAKERELGSQRNSDSGAGTDALADALRRALAARGNAIHSDEDETESSDNEGEWD
Protein: Probable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (ETF-QO) (ETF-ubiquinone oxidoreductase) (EC 1.5.5.1) (Changed intracellular redox state protein 2) (Electron-transferring-flavoprotein dehydrogenase) (ETF dehydrogenase) (Q08822)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Accepts electrons from ETF and reduces ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Probable electron transfer flavoprotein subunit alpha, mitochondrial
- Probable electron transfer flavoprotein subunit beta
- D-lactate dehydrogenase [cytochrome] 1, mitochondrial
Sequence:
MIKFTNENLIRGIRMTISAKSRHLALGTDMTRKFSLSCRFLNKANLTEEEKELLNEPRARDYVDVCIVGGGPAGLATAIKLKQLDNSSGTGQLRVVVLEKSSVLGGQTVSGAILEPGVWKELFPDEKSDIGIPLPKELATLVTKEHLKFLKGKWAISVPEPSQMINKGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVKGVITKDAGISKSGKPKETFERGMEFWARQTVLAEGCHGSLTKQALAKYDLRKGRQHQTYGLGIKEVWEVKPENFNKGFAAHTMGYPLTNDVYGGGFQYHFGDGLVTVGLVVGLDYKNPYVSPYKEFQKMKHHPYYSKVLEGGKCIAYAARALNEGGLQSVPKLNFPGGVLVGASAGFMNVPKIKGTHTAMKSGLLAAESIFESIKGLPVLEEVEDEDAKMAMFDKEATINLESYESAFKESSIYKELYEVRNIRPSFSGKLGGYGGMIYSGIDSLILKGKVPWTLKFDEKNDGEILEPASKYKPIEYPKPDGVISFDILTSVSRTGTYHDDDEPCHLRVPGQDMVKYAERSFPVWKGVESRFCPAGVYEFVKDEKSPVGTRLQINSQNCIHCKTCDIKAPRQDITWKVPEGGDGPKYTLT
Protein: Disintegrin and metalloproteinase domain-containing protein 7 (ADAM 7) (Epididymal apical protein I) (EAP I) (Q63180)
Organism: Rattus norvegicus (Rat)
Function: May play an important role in male reproduction including sperm maturation and gonadotrope function. This is a non catalytic metalloprotease-like protein (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zinc finger protein 511
- Lipocalin 9
Sequence:
MFPTGIFLMSVLISQMQGRGIVGVEGQELVHPKKLSLLQKRDLERIHDSDTPEEYEEELLYEIKLGRKTLTLHLLKAREFLALNYSETYYNIKREMVTRHPQILDHCFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDEGDHLVFKYNVKAPYATNYSCEGLNFTKKSTLIDAKIIEEHKVEDYHKEKFIELFVVADEFVYRRNSKPQNKLRKRIWGMVNFVNMIYKALNIRVTLTGMEIWSAGDEIEIVSNLESTLLHFSTWQETVLKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHDDFPCTCPLGKCVMGAGSIPAIKFSKCSQTQYQQFLKNQKPACILNNPLPEEFNDYPFCGNKKVDEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGVICRPAKNECDISEVCTGYSPECPKDESQANGFPCKNGEGYCFMGLCPTRDDQCAELFSGGAEESHSLCYRMNQKGNRFGYCKNKDNTFVPCEEKDLKCGKIYCTGGRRSAHLGEDKTYNLKNVKQNISIKCKTMFLYHNSRDMGLVNSGTKCGEGMVCSNGECIEMEKAYNSTICSSLCDENDVDDNEPDCQCEEGPIITEWGEALNLTSVSIMVVVLVMVIIGVGLVILLIRYQKCIKMKQVQSSSREIRGIENKVYFPDEHQTRSEPIFTDIYPLHNTAESLERVPSTFSSPHYITLKSVSKDPRGIADPKQNDNMNLNLDSQSDCTRLG
Protein: [histone H3]-lysine(36) N-trimethyltransferase (EC 2.1.1.359) (SET domain-containing protein 2) (A0A0G2KB10)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone H3.1
- Histone H3
- Protein IWS1 homolog
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase subunit beta
- PHD finger protein 3
- Protein polybromo-1
- Histone-lysine N-methyltransferase ASH1L
- [histone H3]-trimethyl-L-lysine
Sequence:
MRLEHFGVLFLREEENEAKIENVQKTGFIKGPIFKGVASSRFLPKGTKTKVNLEEQGRQKVSFSFSLTKKTLQNRFFTALSNEKQSDSPHSPATPQVDSNPKAKMEAGDTFPATEESSPPKSRVELGRIHFKKHLLHVTSRPQLATTTTVASLLPPTTQLPVAIAESTVDSPPSSPPPPPPPPQVSSPSPPAPISEPVALPHPPVTALMTSTPGPLPVDAAVRAQKEPPMKSVPESLELDMKQDIVSNSLEEHTNQTLKEQADNALQKEDSHIGKEEEVSDGSKISLSSKKASSKKKSSQFEGTFLGSESDEDSVRTSSSQRSHDLKSSTSIEKERDFKKSSAPSKSEDLGKSSRSKTERDDKYFSYSKLERDTRYVSTRCRSERDRRRSRSRSRSDRVSRTSLSYSRSERSHYYDSERRYHRSSPYRERTRYSRPYTDNRARESSDSEDEYKKTYPRRTSAHSYRDLRTSSSYSKFDRDCKTETSYLEMERRGKYSSKLERESKRTSEHEAIKRCCSPPNELGFRRGSSYSKHDNNSTSRYKSALSKSISKSDKFKNSFCCTELNEENKQSHSFSLQTPCSKGSELRTINKIPEREKTGSPSPSNQLNDSPTFKKLDESPILKPEFIGHDSHESIKELELPKMKNDQLRNFCSIELNVNGSPETETDVATFRTSKPDAISMTSDDSVTGSEVSPLIKGCVLSSNGFQSVGRCRERDADDACRQHNKSKSPFRETEPLLSPHHDKVMSLPVKTIDYSKTLIKEPVDKRHSCCKTKDSDRYCSPNESSEAENREISSNCFVNVHLDSKTVVCDNRELTDQHSEFTCDGYKQSIGSTSSASLNHFDDLYESVGSSGISSLQSLPSGIRCEENTSPALDTVQSKKGIDFLKYVGKETDVVSALPDSGKAFSSWENRHNMLSGQSLQESQEEGSSTLHERRGRSEVSLDEEEQRGHTHISDDSEVVFPYDLNLTMEDSDGVTYTLKCDSSGNAPEIVSTVHGDYSASSASSSDESDSEDTESDDSSIPRNRLQSVVVVPKNSTLPMEETSPCSSRSSQSYRHYSDHWEDGLESRRHAYEEKFESMASKGCSQTEKFFLHKGTERNPETSYSQFSRKIDNHLPEIAHSQSDGVDSTSHTDVKSDSVGHLNSEDAIRAKMSRPQELPVYCDDFEDLPNTSRQQMIFSNRPDSSRLGKAELSFSSSCDISRMDGLHSSEELRNLGWDFSQQERPTTTYQQPDSSYGTCGTHKYQQSAEHYGGTHDYWQGNGYWDPRSAGRPPGTGVVYDRIQGQVPDSLTDDREEEENWDQRSGSHFSSPSNKFFFHQKDKGSVQAPEISSNSIKDSLVINERKDFSKNFEKNDIKERGPPKKRRQELESDSESDGELQARKKVRVEIEQGQSSVPQHSELVGPSCAMDDFRDPQRWKEFAKLGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEVACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVLSLSRLMVRIETLEQKLTCLKLIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEIIKTLEHLPIPTKNMLEESKVLPIIQRWSQTKTAVPQLSEGDGYSSENTSRAHTPLNTPDPSAKPSTEVDTDTPKKLIFRRLKIISENSMDSAVSDVTSELECKDGKEDLDQLETVTVEEDEELQSQQLLPSQLCESKVESESTIDVSKLPISEPEADTETEPKDSNGTKLEETIAEETPSQDEEEGVSDVESERSQEPPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKESTVTERGRDTAAFRDQTAPKTPNRSREREPDKQSQNKEKRKRRGSLSPPSSAYERGTKRPDDRYDTPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPFDSLGYNASHHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHAQPLVGHSTESLAAPPSVPVVPHGAASVEVSSSQYAAQSESVVHQDSSVPGMPVQTPGPVQGQNYSVWDSNQQSVSVQPQYSPAQSQATIYYQGQTCSTVYGVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAHPQGVVVQPAAAVTTIVAPGQPQPLQPPEMVVTNNLLDLPPPSPPKPKTIVLPPNWKTARDPEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKTSKKPKTAEADTSSELAKKSKEVFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKELKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE
Protein: Mitochondrial inner membrane protein OXA1 (Oxidase assembly 1 protein) (AtOXA1) (Q42191)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for activity and assembly of cytochrome c oxidase.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11148275}; Multi-pass membrane protein {ECO:0000269|PubMed:11148275}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial import inner membrane translocase subunit TIM50
- Signal recognition particle 43 kDa protein, chloroplastic
- Preprotein translocase subunit SCY1, chloroplastic
- Sec-independent protein translocase protein TATA, chloroplastic
- Signal recognition particle subunit SRP54, chloroplastic
- Cytochrome c oxidase subunit 2
- Mitochondrial intermembrane space import and assembly protein 40 homolog
- Mitochondrial import inner membrane translocase subunit TIM9
- FAD-linked sulfhydryl oxidase ERV1
Sequence:
MAFRQTLSIRSRLFARRNQPVYHIIPRESDHERDSFCQETSQRSYHSFLHQRSVNNSDFSKVSGGSLHLPLAPTSGFAFYRYMSSAPGVGSEKIGVMSDIAEVITDSTLQDVPAQAAAAVSEVTLAAADSFFPIAALQQCIDMVHTFTGFEWWASIVVATILIRSSTVPLLIKQMKDTTKLALMRPRLESIREEMQNKGMDSVTMAEGQKKMKNLFKEYGVTPFTPMKGMFIQGPLFICFFLAIRNMAEKVPSFQTGGALWFTDLTTPDSLYILPVITGLTFLITVECNAQEGMEGNPMAGTVKTVCRVFALLTVPMTMSFPQAIFCYWITSNLFSLMYGLVIKRPQVKKMLRIPDLPPPPPGQQPSFDLFSALKKMKAMTQDHTQNQIEPPSPVNPRLSSTSLSPVSKRLKALESQVKGRKKNSSKKK
Protein: Bleomycin hydrolase (EC 3.4.22.40) (A8JV22)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR005700}.
Interaction partners:
Sequence:
MYYSKESVQTHTISGERCQSHLLAADNNSGSGGGGSGGGGAGNNNSANSGKNSTHRFAETSVITNQLLEKWRKNFYSEPKNLLAQNVCSRVDPFDVCLSRKALETTNHVFNYKVETEGKPVTNQRSSGRCWLFAALNCIRLPFMKNYNLDEFEFSQAFLFYWDKIERCNYFLNNVVKTAQRGEKVDGRLVSFLLLDPTSDGGQWDMLVNLITKHGLMPKKCFPESFSCESSLRMNAILKSKLREYARNLRVLMEKNPTDEEIACKIQEQMAEIYKVVGICLGIPSETFTWEYYDKSKNYQSIGPVSSLEFYERYVKPHFNVEDKVCLVTDPRPTSSYDQAYTVDCLGNVVGGRPVLYNNQSVELLLAVVTKSLKAGEAVWFGCEVSKRFASKQGIEDVDVHDFKLVFDIDIQTTFSKADRLIYGESAMTHAMVFTAVSVDKSGVAQKLRVENSWGEDRGEKGYLVMNADWFREFGFEVVVDKKYVPEDVLRVFDMDPIVLPAWDPMGTLAQ
Protein: IQ motif-containing GTPase-activating protein 2 (Ras GTPase-activating-like protein IQGAP2) (A2CE93)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cell division control protein 42 homolog
- Cell division cycle 42-like 2
- Cell division control protein 42 homolog
- Rac family small GTPase 1a
- Si:ch211-1f22.1.
- Rac family small GTPase 3a)
- Rac family small GTPase 3b
- Rac family small GTPase 2.
- Rac family small GTPase 1b
- IQ motif-containing GTPase-activating protein 1.
Sequence:
MVKPQQSFRGSRMYHEDGANSLRPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWMEACLEEQLPPTTELENGLRNGVYLGKLAKFFAPQLVSEKKIYDRDQSWYKLSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPKVIYCIHALSLYLYKLGIAPQIQDLLGKVDFTEEEISNMRKELEKYGIQMPAFSKIGGILANELSVDEAALHAAVFAINEAIDKGHAENTMTALRNPNALLRNTEKALAQVYQDTLSKAKRKKEDQASGRRSSVATEERDVYEELLTQQEIQSNVDLVNTSSAVQRLHQALEAEDQKALLASLKLPALGLVGVTDENACFYLEHFTSYRQHKDAGLGAQLGKDEIQKVITSCNEFAEAEKRKQEAVVAINSAIRRGIPEETVEELLNPEAQMPIVYHTAASLYQAELFSLQLGSKNKAGLSHEELCVAVEMLSAVSVLNEVLDTKDSVAVIEQLSDSPLGFSGMDADNLQRYTDTLIHLREESLARGQEFLTWNDVQKCIDTVNVQVHEEHERVIAIAEINEALHSGDPEKTLAALLLSTAKLQGVKAANAKHYHDLLLTTKDHICKSSGDESAVLWLDQIQEAIYTANQNQEDALRLAAAVADINRAVCEEDAKATMSALQCPDAGLRAVMPECAQIYQSQLHQLQSTQTQQGTSGSSWVQHKIKDKYDYFYNIECKEGTWVEPEHFVHDSSQLSREDIQNVLSSVTAEYNREQLWLANEPFIIQLQALIRGYLVRRAHQDRLEYLRKQEPSVIKLQASWKGYKQRSVYKERLRTFQDSASTVVKLQSLVKMWRAKRSYTKRLQYFRDHEKEIVKIQAFLKANKARVDYTTLTGSQHPPLSVVRKFVHLLEQSSLDLQEEQDVTRLREEVVTKIRANQQMEKDLNLMDIKIGLLVKNRITLQDVVSHSKKMKSKKNKMSKEDLAMGEKQGIKGLSKEKRKKLEAYQHLFYLLQTNPSYLAKLIFQMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFESALREEIKSKVDHIQEIVTGNPTVIKMVLSFYRGARGQNALRQLLGPVVKEIIEDKNLGINTNPVDIYKAWVNQLETATGEASKLPYEVTPEQALLHEEVRAKLESSNQVLRSVTDKVLGSIMSSLDNIPYGMRYIAKVLKDALHEKFPDATEDELLKIVGTLLYYRYMNPAIVAPDGFDIIDMTAGGQVHSEQRRNLASVAKMLQHAAANKLFEDESDHLTPMNSYISQTYQKFRGFFQAACDVPAPEEKFNVDEYSDMVTLSKPVIYISIEEIINTHSLVLEHKEAIAPDQSDLLHELLKDLGVVPDIESLLGEGTVDTNDLGKENSLSQHGKTEISLTLTNKFELLDGDDKDTKGLMTKTKKLIVDVVRIQPGETLTDILETPASATQEAEHAKLVERQVVQDSQTPEGLKSSQAMLEDRQLPLEQKKRKILRNLRTLEQAGLVNSKHKYQEVINDISKDIRYQRRYRQRRKAELVKLQQTLTALNSKTDFYQEQINYYDTYIKTCLDNLNRNNGYFFIRNSRRSIKLDRKDEEKGSKKSKASSLKYTAAKLHEKGVILEIEGVQINQFKNVMFDICPCEEVGDFEIKAKFMGVEMEKVQLHFQDLLQLQYEGVAVMKMFDKAKVNVNLLIFLLNKKFYGK
Protein: Uncharacterized protein (Q9I547)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Uncharacterized protein
- Phage holin
- Phage holin family protein
- Phage tail protein
- Glycoside hydrolase family 19 protein
- Uncharacterized protein
- N-acetylmuramoyl-L-alanine amidase
- Holin
- Probable bacteriophage protein
- NlpC/P60 domain-containing protein
Sequence:
MSSATVRLDHAALRETLRQLFGLPAGSVIDADQLLAPPAIPFMTLRLESLSLLGKVRREFSASGEQESLLASCESIFRLTWHGPEAHQYLQDARCLLQSGNAGERLRVLKASLLRLTPIENLSVVQDGQALGQARFDLVLAHEHVLLVDLERTAPGQASGGAGGTAS
Protein: Translocation protein SEC62 (Q32PD3)
Organism: Bos taurus (Bovine)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MAERRRHKKRIQEVGEPSKEEKAVAKFLRFNCPTKSTNMMGHRVDYFIASKAVDCLLDSKWAKAKKGEEALFTTRESVVDYCNRLLKKQFFHRALKVMKMKYEKDIKKEKKKKK
Protein: Rhomboid-related protein 2 (RRP2) (EC 3.4.21.105) (Rhomboid-like protein 2) [Cleaved into: Rhomboid-related protein 2, N-terminal fragment (NTF); Rhomboid-related protein 2, C-terminal fragment (CTF)] (Q9NX52)
Organism: Homo sapiens (Human)
Function: Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Known substrate: EFNB3.
Subcellular location: [Rhomboid-related protein 2, C-terminal fragment]: Cell membrane {ECO:0000269|PubMed:19850051}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nicastrin
- Ephrin-B3
- Gamma-secretase subunit PEN-2
- Gamma-secretase subunit APH-1A
- Ephrin-B2
- Presenilin-1
Sequence:
MAAVHDLEMESMNLNMGREMKEELEEEEKMREDGGGKDRAKSKKVHRIVSKWMLPEKSRGTYLERANCFPPPVFIISISLAELAVFIYYAVWKPQKQWITLDTGILESPFIYSPEKREEAWRFISYMLVHAGVQHILGNLCMQLVLGIPLEMVHKGLRVGLVYLAGVIAGSLASSIFDPLRYLVGASGGVYALMGGYFMNVLVNFQEMIPAFGIFRLLIIILIIVLDMGFALYRRFFVPEDGSPVSFAAHIAGGFAGMSIGYTVFSCFDKALLKDPRFWIAIAAYLACVLFAVFFNIFLSPAN
Protein: Shootin-1 (Shootin1) (A0MZ66)
Organism: Homo sapiens (Human)
Function: Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Also plays a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons.
Subcellular location: Perikaryon {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection, axon {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8K2Q9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection, filopodium {ECO:0000250|UniProtKB:A0MZ67}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:A0MZ67}. Note=Localizes in multiple growth cones at neurite tips before the neuronal symmetry-breaking step. Accumulates in growth cones of a single nascent axon in a neurite length-dependent manner during the neuronal symmetry-breaking step; when absent from the nascent axon's siblings, probably due to competitive transport, prevents the formation of surplus axons. Transported anterogradely from the soma to the axon growth cone in an actin and myosin-dependent manner and passively diffuses back to the cell bodies. Colocalized with L1CAM in close apposition with actin filaments in filopodia and lamellipodia of axonal growth cones in hippocampal neurons. Exhibits retrograde movements in filopodia and lamellopodia of axonal growth cones. Colocalized with KIF20B along microtubules to the tip of the growing cone in primary hippocampal neurons. Recruited to the growth cone of developing axon in a KIF20B- and microtubule-dependent manner. {ECO:0000250|UniProtKB:A0MZ67, ECO:0000250|UniProtKB:Q8K2Q9}.
Interaction partners:
- Neural cell adhesion molecule L1
- Protein RUFY3
- E3 ubiquitin-protein ligase LNX
Sequence:
MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDEDSTTDTDGAAETCVSVQCQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQAVEEMMDRIKKGVHLRPVNQTARPKTKPESSKGCESAVDELKGILGTLNKSTSSRSLKSLDPENSETELERILRRRKVTAEADSSSPTGILATSESKSMPVLGSVSSVTKTALNKKTLEAEFNSPSPPTPEPGEGPRKLEGCTSSKVTFQPPSSIGCRKKYIDGEKQAEPVVVLDPVSTHEPQTKDQVAEKDPTQHKEDEGEIQPENKEDSIENVRETDSSNC
Protein: Sorting nexin-14 (Q8BHY8)
Organism: Mus musculus (Mouse)
Function: Plays a role in maintaining normal neuronal excitability and synaptic transmission. May be involved in several stages of intracellular trafficking. Required for autophagosome clearance, possibly by mediating the fusion of lysosomes with autophagosomes. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), a key component of late endosomes/lysosomes. Does not bind phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q9Y5W7}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Y5W7}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:24859318}.
Interaction partners:
- Sorting nexin-13
Sequence:
MWLRRRGLGVPSASASEGGTSSPAWTEMGSWVRTICGRLKQRLRLDVGREICRQYPLFCFLLLCLSVASLLLNRYLHVLMIFWSFVAGVVTFYCSLGPDSLLPNIFFTIKYKPKQLGLQELFPQGHSCAVCGKVKCKRHRPSLLLENYQPWLDLKVSSKVDASLSEVLELVLENFVYPWYRDVTDDESFVDELRITLRFFASVLVRRIHKVDIPSIITKKLLKAAMKHIEVIVKARQKVKNTEYLQQAALEEYGPELHVALRSRRDELQYLRKLTELLFPYILPPKATDCRSLTLLIREILSGSVLLPSLDFLADPDTVNHLLIIFIDDSPPEKATEPASPLVPFLQKFAEPRNKKPSVLKLELKQIREQQDLLFRFMNFLKQEGAVHVLQFCLTVEEFNDRILRPELSNDEMLSLHEELQKIYKTYCLDESIDKIRFDPFIVEEIQRIAEGPYIDVVKLQTMRCLFEAYEHVLSLLENVFTPMFCHSDEYFRQLLRGAESPTRNSKFNRSTQKRGESFGISRIGSKIKGVFKSTTMEGAVLPNYGVAEGEDDFIEEGIVVMEDDSPVEAVSTPNTPRNLAAWKISIPYVDFFEDPSSERKEKKERIPVFCIDVERNDRRAVGHEPEHWSVYRRYLEFYVLESKLTEFHGTFPDAQLPSKRIIGPKNYEFLKSKREEFQEYLQKLVQHPELSNSQLLADFLSPNGGETQFLDKILPDVNLGKIIKSVPGKLMKEKGQHLEPFIMSFINSCESPKPKPSRPELTILSPTSENNKKLFNDLFKNNANRAENTERKQNQNYFMEVMTVDGVYDYLMYVGRVVFQVPDWLHHLLMGTRILFKNTLEMYTDYYLQCKLEQLFQEHRLVSLITLLRDAIFCENTEPRSLQDKQKGAKQTFEEMMNYIPDLIVKCIGEETKYESIRLLFDGLQQPVLNKQLTYVLLDIVIQELFPELNKVQKEATSMTSWM
Protein: Interferon-inducible double-stranded RNA-dependent protein kinase activator A (Protein activator of the interferon-induced protein kinase) (Protein kinase, interferon-inducible double-stranded RNA-dependent activator) (Q4V8C7)
Organism: Rattus norvegicus (Rat)
Function: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association, sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Endoribonuclease Dicer
- Protein argonaute-1
- RISC-loading complex subunit TARBP2
- Protein argonaute-2
- Ribonuclease 3
- Interferon-induced, double-stranded RNA-activated protein kinase
- Protein argonaute-4
- Protein argonaute-3
- Microprocessor complex subunit DGCR8
- Exportin-5
Sequence:
MSHSRHRAEAPPLQREDSGTFSLGKMITAKPGKTPIQVLHEYGTKTKNIPVYECERSDVQVHVPTFTFRVTVGDITCTGEGTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYTTICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSLPNTDYIQLLSEIAKEQGFSITYLDIEELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
Protein: Coiled-coil domain containing 14 (A0A0A0MR27)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVRSGARPGQVLSSGRHTGPAKLTNGKKATYLRKIPRFNADSGYSIHSDSESQAETVHGLDGCASLLRDILRNEDSASSDNKKQIPNEASARSERDTSDLEQNWSLQDHYRMYSPIIYQALCEHVQTQMSLMNDLTSKNIPNGIPAVPCHAPSHSESQATPHSSYGLCTSTPVWSLQRPPCPPKVHSEVQTDGNSQFASQGKTVSATCTDVLRNSFNTSPGVPCSLPKTDISAIPTLQQLGLVNGILPQQGIHKETDLLKCIQTYLSLFRSHGKETHLDSQTHRSPTQSQPAFLATNEEKCAREQIREATSERKDLNIHVRDTKTVKDVQKAKNVNKTAEKVRIIKYLLGELKALVAEQEDSEIQRLITEMEACISVLPTVSGNTDIQVEIALAMQPLRSENAQLRRQLRILNQQLREQQKTQKPSGAVDCNLELFSLQSLNMSLQNQLEESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKDKDQTILENKQQYDIEITRIKIELEEALVNVKSSQFKLETAEKENQILGITLRQRDAEVTRLRELTRTLQTSMAKLLSDLSVDSARCKPGNNLTKSLLNIHDKQLQHDPAPAHTSIMSYLNKLETNYSFTHSEPLSTIKNEETIEPDKTYENVLSSRGPQNSNTRGMEEASAPGIISALSKQDSDEGSETMALIEDEHNLDNTIYIPFARSTPEKKSPLSKRLSPQPQIRAATTQLVSNSGLAVSGKENKLCTPVICSSSTKEAEDAPEKLSRASDMKDTQLLKKIKEAIGKIPAATKEPEEQTACHGPSGCLSNSLQVKGNTVCDGSVFTSDLMSDWSISSFSTFTSRDEQDFRNGLAALDANIARLQKSLRTGLLEK