wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-1A adrenergic receptor (Alpha-1A adrenoreceptor) (Alpha-1A adrenoceptor) (Alpha-1C adrenergic receptor) (P43140)
Organism: Rattus norvegicus (Rat)
Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity).
Subcellular location: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-11
- Alpha-1D adrenergic receptor
- Guanine nucleotide-binding protein subunit alpha
Sequence:
MVLLSENASEGSNCTHPPAPVNISKAILLGVILGGLIIFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGVRALLCVWVLSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYVPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNVPAEGGGVSSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLRRRQSSKHALGYTLHPPSQALEGQHRDMVRIPVGSGETFYKISKTDGVCEWKFFSSMPQGSARITVPKDQSACTTARVRSKSFLQVCCCVGSSAPRPEENHQVPTIKIHTISLGENGEEV
Protein: Carbonic anhydrase 14 (A0A8I6AHH2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
KGYLNPEITTGSPKDTPSVKGHLSSDSSSPRTQALCLFPLPLIQLHWSETTGPHGQDHWPASYPECGGNAQSPIDIQTDGVIFDPDLPTVQPHGYDQLGTEPLDLHNNGHTVQLSLPPTLHLGGLPRKYTAAQLHLHWGQKGTLKGSEHQINSEATAAELHVVHYDSESYGSLSEAAQKPQGLAVLGILIEVGETENPAYDHILSHLHEVRYKDQKTSVPPFNVRELLPQQLEQFFRYNGSLTTPPCYQSVLWTVFNRRAQISMGQLEKLQETLSSTEEDPSEPLVQNYRVPQPLNQRTIFASFIQVGPLYTTGEMLGLGMGISAGCLCLLLTIYFIAQKIRRKRLGNRKSVVFTSARATTEA
Protein: Calcium-activated chloride channel regulator 3A-1 (EC 3.4.-.-) (Q9QX15)
Organism: Mus musculus (Mouse)
Function: Plays a role in modulating chloride current across the plasma membrane in a calcium-dependent manner.
Subcellular location: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Anoctamin-2
- Anoctamin-1
- Zymogen granule membrane protein 16
- Cystic fibrosis transmembrane conductance regulator
Sequence:
MVPGLQVLLFLTLHLLQNTESSMVHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILVPMTWKSKPEYLMPKRESYDKADVIVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHLRWGVFDEYNVDQPFYMSRKNTIEATRCSTRITGTNVVHNCERGNCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFMQNLNSVVEFCTEKNHNAEAPNLQNKMCNRRSTWDVIKTSADFQNAPPMRGTEAPPPPTFSLLKSRRRVVCLVLDKSGSMDKEDRLIRMNQAAELYLTQIVEKESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQASGGTSICHGLQAGFQAITSSDQSTSGSEIVLLTDGEDNGIRSCFEAVSRSGAIIHTIALGPSAARELETLSDMTGGLRFYANKDLNSLIDAFSRISSTSGSVSQQALQLESKAFDVRAGAWINGTVPLDSTVGNDTFFVITWMVKKPEIILQDPKGKKYTTSDFQDDKLNIRSARLQIPGTAETGTWTYSITGTKSQLITMTVTTRARSPTMEPLLATAHMSQSTAQYPSRMIVYARVSQGFLPVLGANVTALIEAEHGHQVTLELWDNGAGADTVKNDGIYTRYFTDYHGNGRYSLKVRVQAQRNKTRLSLRQKNKSLYIPGYVENGKIVLNPPRPDVQEEAIEATVEDFNRVTSGGSFTVSGAPPDGDHARVFPPSKVTDLEAEFIGDYIHLTWTAPGKVLDNGRAHRYIIRMSQHPLDLQEDFNNATLVNASSLIPKEAGSKETFKFKPETFKIANGIQLYIAIQADNEASLTSEVSNIAQAVKLTSLEDSISALGDDISAISMTIWGLTVIFNSILN
Protein: Nicalin (Inactive aminopeptidase nra-2) (Nicotinic receptor-associated protein 2) (A5JYX8)
Organism: Caenorhabditis elegans
Function: Involved in the recognition and selection of protein complexes to exit the endoplasmic reticulum (ER). In muscles, regulates levamisole-sensitive nicotinic acetylcholine receptor (L-AChR) subunit composition, possibly by allowing only specific L-AChR subunit combinations to exit the ER. Specifically, may promote the inclusion of alpha subunits unc-38 and unc-29 into L-AChR. Regulates L-AChR sensitivity to agonists such as nicotine and levamisole at neuro-muscular junctions. In touch neurons, may prevent ER exit of incorrectly folded mec-4-mec-10 ion channel.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19609303}; Single-pass type I membrane protein {ECO:0000255}. Note=During the assembly of acetylcholine receptor in muscles, colocalizes with L-AChR component unc-29 in the ER. {ECO:0000269|PubMed:19609303}.
Interaction partners:
- Nicotinic receptor-associated protein 4
- PAT complex subunit CCDC47
- Calcium load-activated calcium channel homolog
- Translocon Sec61/SecY plug domain-containing protein
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL19
- BOS complex subunit TMEM147
- Uncharacterized protein
- Nicotinic receptor-associated protein 1
- Protein transport protein Sec61 subunit beta
Sequence:
MQDEIIDFFRSPALLFYMTLMLTICVVNGSQQVGEVVETEFHAYRLHQYEISGNIYGCKNYRVSYEAVSLGARTLRRTMVTTWRDLLTTDVDDMWALSTGAVLIFIPDNLDELNDIDRKAFIDLEAKLLSAKTDLAVYVAPFNDDAVSILHDVNTRSEKAPTALQHLLQSLSGNTISITSSDQSPELPPSYKPLNIVGRLSSGDRAAPTIAFVAHYDTQSAVPGVSPGADSNGSGIVALLELLAVLSKFYDSPSTRPPYNILFIWTAAGKLNYQGTRHWIDEYQKGFDSADYAKSGLSRKGFSDDRVDLAICIEAIGRKTGGFFMHAGKTPSENSVAAQLLRRLKYFSSISPKKNIELVTKKISLTTVSAWEHEKFNIKRMPAITLSTLPSPSDPARNSILDLPSALDEDELIDNIRLIGEAVLGYILDLPESGPSSDSRVKSEATMLSKDAVDKQRVHHFIRQFASRPRPVGDQRATESITSNLASVAAGYGNVFKSAVTITDAKAFGVTQNRLVAERVKPAVFELVIAAGVFTYLSAFYYIATHSQNTIEGTVAAIRKSIF
Protein: Protein LSM14 homolog A (Protein FAM61A) (RNA-associated protein 55A) (mRAP55A) (Q8K2F8)
Organism: Mus musculus (Mouse)
Function: Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for translationally inactive mRNAs and protect them from degradation. Acts as a repressor of mRNA translation. May play a role in mitotic spindle assembly.
Subcellular location: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q8ND56}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8ND56}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8ND56}.
Interaction partners:
- Probable ATP-dependent RNA helicase DDX6
- Eukaryotic translation initiation factor 4E transporter
- Enhancer of mRNA-decapping protein 3
- m7GpppN-mRNA hydrolase
- Polyadenylate-binding protein 1
- Eukaryotic translation initiation factor 4E
- Protein PAT1 homolog 1
- KIF-binding protein
- Fragile X messenger ribonucleoprotein 1
- U6 snRNA-associated Sm-like protein LSm1
Sequence:
MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDEVFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSSSSFQSVGSYGPFGRMPAYSQFSPSTLVGQQFGAVGVAGNSLTSFGTEASNSGTLSQSNAVGSAFTQDTRSVKPQLAQGRSSPQLDPLRKSPTMEQAVQTASAHLPAPAPVGRRSPVPARPLPPTSQKAIDNQEHRRAEVHKVPRPENEQLRNDKRQVVPGVPSAPRRGRGGHRGGRGRFGIRRDGPMKFEKDFDFESANAQFNKEEIDREFHNKLKLKEDKLEKQEKPVNGEDKGDSGVDTQNSEGNADEEDPLGPNCYYDKTKSFFDNISCDDNRERRPTWAEERRLNAETFGIPLRPNRGRGGYRGRGGLGFRGGRGRGSGRGGTFTAPRGFRAGFRGARGGREFADFEYRKTTAFGP
Protein: 3'-5' RNA helicase YTHDC2 (EC 3.6.4.13) (YTH domain-containing protein 2) (hYTHDC2) (Q9H6S0)
Organism: Homo sapiens (Human)
Function: 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells. Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability. Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (By similarity). Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease. Required for both spermatogenesis and oogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:B2RR83}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29970596}.
Interaction partners:
- 5'-3' exoribonuclease 1
- Meiosis-specific coiled-coil domain-containing protein MEIOC
- N
- Zinc finger CCCH domain-containing protein 13
- N
- Pre-mRNA-splicing regulator WTAP
- RNA demethylase ALKBH5
- Protein virilizer homolog
- Cleavage and polyadenylation specificity factor subunit 5
- RNA-binding protein 15
Sequence:
MSRPSSVSPRQPAPGGGGGGGPSPCGPGGGGRAKGLKDIRIDEEVKIAVNIALERFRYGDQREMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKKKDGSETAHAMMTCNLTHNTKHAVRSLIQRFPVTNKERTELLPKTERGNVFAVEAENREMSKTSGRLNNGIPQIPVKRGESEFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFIRYFGSCPVIYIQGRPFEVKEMFLEDILRTTGYTNKEMLKYKKEKQQEEKQQTTLTEWYSAQENSFKPESQRQRTVLNVTDEYDLLDDGGDAVFSQLTEKDVNCLEPWLIKEMDACLSDIWLHKDIDAFAQVFHLILTENVSVDYRHSETSATALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSATLEFGNLDESSLVQTNGSDLSAEDRELLKAYHHSFDDEKVDLDLIMHLLYNICHSCDAGAVLIFLPGYDEIVGLRDRILFDDKRFADSTHRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLAPVNCPIADFLMKAPEPPPALIVRNAVQMLKTIDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKRAAMLCRKRFTAGAFSDHMALLRAFQAWQKARSDGWERAFCEKNFLSQATMEIIIGMRTQLLGQLRASGFVRARGGGDIRDVNTNSENWAVVKAALVAGMYPNLVHVDRENLVLTGPKEKKVRFHPASVLSQPQYKKIPPANGQAAAIKALPTDWLIYDEMTRAHRIANIRCCSAVTPVTILVFCGPARLASNALQEPSSFRVDGIPNDSSDSEMEDKTTANLAALKLDEWLHFTLEPEAASLLLQLRQKWHSLFLRRMRAPSKPWSQVDEATIRAIIAVLSTEEQSAGLQQPSGIGQRPRPMSSEELPLASSWRSNNSRKSSADTEFSDECTTAERVLMKSPSPALHPPQKYKDRGILHPKRGTEDRSDQSSLKSTDSSSYPSPCASPSPPSSGKGSKSPSPRPNMPVRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSIVYLVFSVQGSGHFQGFSRMSSEIGREKSQDWGSAGLGGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPLVGEQLLQLWERLPLGEKNTTD
Protein: Exocyst complex protein EXO70 (Q5AH25)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Also plays a role in the assembly of the exocyst (By similarity).
Subcellular location: Bud {ECO:0000250}. Bud neck {ECO:0000250}.
Interaction partners:
- Exocyst complex component SEC15
- Exocyst complex component SEC5
- SNARE-binding exocyst subunit
- Exocyst subunit
- Exocyst complex component EXO84
- Exocyst complex component Sec8
- Rcy1p
- Ras-related protein SEC4
- GTP-Rho binding exocyst subunit
- GTP-binding protein RHO3
Sequence:
MSYNLDVDEADVAVLNQNLIRSKELFESIGKSLHKISTKSQTASSTINPVLKQVNQLTTNKHEVENGLKLLQEVSENASKINDLENLLNNSIENSPGGIKSYLINLNQSKNLLSQIKTQSKFKQFKGILYNFENLIDRSETKVQKYYQDLINGKDSRAIIDKRDEIKLIFQYFSNPQTKSTSNSGGNEEYVTKLYVRARSKRLIEKLKPIESSTKPAVKANANIPYEKGTNGITKYTDVLSGEIEQELIILNECQLSTHLIGPIVEESISRYNGIINKYNQVYFKTPQEIVDNVILILEVLNNLIDFKVKLKQIGLNRTLEQSNFINTFEQYLETNSVIFKEFIQAIDNRFQNLGKFNEINTQEVIVELMSKLRRLSEFKLALLQLIKNYSIGQWLVSQPPMRFVNVFSSVIPNSQPQANSDGEEDEVIQEYLLSSFYSDVIDAIMINIEIGLKKNTSGGDSLPSSSSTSASTNATSGTSSLSLNKKSTQGFILIKNLFMLESIVNRSQYLYQSLGSLGEERILRLKNRFLKLFLDDWSHASYIIIRDMTTIATQSAQHQQSQQQSSNTIGTGGGTVTNLSNKEKDQVKDLFKNFNESFEEALFNYQKYNFGDAILKKYLSNEIKKLILNTYFKLYDKYGNSDFTKNKSKYVKYDKLNFEKLLNERL
Protein: Perilipin (F6QBA3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Hormone-sensitive lipase
- Heat shock cognate 71 kDa protein
- Perilipin-1
- Perilipin-5
- Patatin-like phospholipase domain-containing protein 2
- Butyrophilin, subfamily 1, member A1
- Erythroblast membrane associated protein
- Butyrophilin, subfamily 2, member A2
- Butyrophilin-like 9
Sequence:
MASVAVDPQPSVVTRVANLPLVSSTYDLVSSAYVSTKDQHPYLRSVCEMAEKGVRTVTSVAVTGALPIIQKLEPQIAVANTYACKGLDRMEARLPILNQPTSEIVANARGAVTGAKDVVTTTMAGAKDSVASTVSGVVDKTKGAVTGSVERTKSVVNGGIDTVLGMLLVDQYLPLTQKELEMEAKKVEGFDMVQKQRYYERLESLSTKICTRAYHQALGRIKDAKQKGQETISQLHSTVHLIEFARKNVHSANQKIQDKLSVSWVEWKRIVGYDDTDESHCAEHIESHTLSMARNLTQQLHTTCQTLLFNVQGLPQNIQDQAKHLGVMAGDIYSAFRNVTSFKEVSDGVLTSSKGQLQKMKESLDEVMDYLVNNTPLNWLMLDFSAFDSTSDTDEVPDIIPLEED
Protein: Disintegrin acostatin-alpha [Cleaved into: Disintegrin acostatin-alpha, processed form] (Q805F7)
Organism: Agkistrodon contortrix contortrix (Southern copperhead)
Function: Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits ADP-induced platelet aggregation in human platelet-rich plasma.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MIQVLLVTLCLAVFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAIQPKNPCCDAATCKLTPGSQCAEGLCCDQCKFIKAGKICRRARGDNPDYRCTGQSGDCPRKHFYA
Protein: Serine protease inhibitor Rv3364c (O50393)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Effector protein that binds to the host serine protease cathepsin G on the macrophage cell membrane, inhibiting its enzymatic activity and the downstream activation of caspase-1-dependent apoptosis. Thus prevents macrophage pyroptosis and helps M.tuberculosis survival within host cells.
Subcellular location: Secreted {ECO:0000269|PubMed:22275911}. Host cytoplasm {ECO:0000269|PubMed:22275911}. Note=Is translocated into the cytoplasm of macrophages. {ECO:0000269|PubMed:22275911}.
Interaction partners:
- Probable ATP/GTP-binding protein
- DUF742 domain-containing protein
- histidine kinase
- Pentapeptide repeat protein MfpA
- DUF732 domain-containing protein
- Beta-lactamase
Sequence:
MKARLPDSPLDWLVSKFAREVPGVAHALLVSVDGLPVAASEHLPRERADQLAAVTSGLASLAGGAAQLFDGGQVLQSVVEMQNGYLLLMQVGDGSALAALAATGCDIGQIGYEMAILVERVGGVVQSCRR
Protein: 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31) (O95336)
Organism: Homo sapiens (Human)
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- 6-phosphogluconate dehydrogenase, decarboxylating
- GDH/6PGL endoplasmic bifunctional protein
- Probable gluconokinase
- Exosome complex component RRP4
- Transaldolase
- N-acetylglucosamine-6-phosphate deacetylase
- N-acetylglucosamine-6-phosphate deacetylase
- Glucose-6-phosphate isomerase
- Ribose-5-phosphate isomerase
Sequence:
MAAPAPGLISVFSSSQELGAALAQLVAQRAACCLAGARARFALGLSGGSLVSMLARELPAAVAPAGPASLARWTLGFCDERLVPFDHAESTYGLYRTHLLSRLPIPESQVITINPELPVEEAAEDYAKKLRQAFQGDSIPVFDLLILGVGPDGHTCSLFPDHPLLQEREKIVAPISDSPKPPPQRVTLTLPVLNAARTVIFVATGEGKAAVLKRILEDQEENPLPAALVQPHTGKLCWFLDEAAARLLTVPFEKHSTL
Protein: Zinc finger protein 224 (Bone marrow zinc finger 2) (BMZF-2) (Zinc finger protein 233) (Zinc finger protein 255) (Zinc finger protein 27) (Zinc finger protein KOX22) (Q9NZL3)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation as a transcriptional repressor. The DEPDC1A-ZNF224 complex may play a critical role in bladder carcinogenesis by repressing the transcription of the A20 gene, leading to transport of NF-KB protein into the nucleus, resulting in suppression of apoptosis of bladder cancer cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:12239212, ECO:0000269|PubMed:20587513, ECO:0000269|PubMed:23665872}. Note=Colocalizes with DEPDC1A at the nucleus.
Interaction partners:
- Fructose-bisphosphate aldolase A
- DEP domain-containing protein 1A
- Fructose-bisphosphate aldolase
- Transcription intermediary factor 1-beta
- Protein arginine N-methyltransferase 5
Sequence:
MTTFKEAMTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLSVGHQAFHRDTFHFLREEKIWMMKTAIQREGNSGDKIQTEMETVSEAGTHQEWSFQQIWEKIASDLTRSQDLMINSSQFSKEGDFPCQTEAGLSVIHTRQKSSQGNGYKPSFSDVSHFDFHQQLHSGEKSHTCDECGKNFCYISALRIHQRVHMGEKCYKCDVCGKEFSQSSHLQTHQRVHTGEKPFKCVECGKGFSRRSALNVHHKLHTGEKPYNCEECGKAFIHDSQLQEHQRIHTGEKPFKCDICGKSFCGRSRLNRHSMVHTAEKPFRCDTCDKSFRQRSALNSHRMIHTGEKPYKCEECGKGFICRRDLYTHHMVHTGEKPYNCKECGKSFRWASCLLKHQRVHSGEKPFKCEECGKGFYTNSQCYSHQRSHSGEKPYKCVECGKGYKRRLDLDFHQRVHTGEKLYNCKECGKSFSRAPCLLKHERLHSGEKPFQCEECGKRFTQNSHLHSHQRVHTGEKPYKCEKCGKGYNSKFNLDMHQKVHTGERPYNCKECGKSFGWASCLLKHQRLHSGEKPFKCEECGKRFTQNSQLHSHQRVHTGEKPYKCDECGKGFSWSSTRLTHQRRHSRETPLKCEQHGKNIVQNSFSKVQEKVHSVEKPYKCEDCGKGYNRRLNLDMHQRVHMGEKTWKCRECDMCFSQASSLRLHQNVHVGEKP
Protein: TBC1 domain family member 1 (A0A8I5ZLK4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEAITFTARKHPFPNEVSVDFGLQLVGSLPVHSLTTMPMLPWVVAEVRRLSGQCSKKEPGMKQVRLWVSPSGLRCEPDLRKSQPWDPLICSSIFECKPQRVHKLIHNSQDPSYFACLIKEDAAHQQSLCYVFKADDQTKVPEIISSIRQAGKIARQEELRCPSEFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRRIDWDAPTGQPSAPGARPMRKSFSQPGLRSLAFRKEFQDASLRSSTFSSFDNDIENHLIGGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGGGAGFHFVCYVFQCTNEALVDEIMMTLKQAFTVAAVQQTAKAPAQLCEGCPLQGLHKLCERIEGMNSSKTKLELQKHLTTLTNQEQAMIFEEVQKLRPRNEQRENELIISFLRCLYEEKQKEHSHTGEPKQTLQVAAENIGSELPPSASRFRLDSLKNRAKRSLTESLESILSRIASPTSHSPFPCHISNLLSEALPISESSFKLLGSSDDLSSDSESHIAEESALLSPQQAFRRRANTLSHFPVECPAPPEPAQTSPGVSQRKLMRYHSVSTETPHERNVDHLPGGESRCCPGQPSDPPPLPPRLNPSASSPNFFKYLKHNSSGEQSGNAVPKSVSYRNALRKKLHSSSSVPNFLKFLAPVDENNTCDFKNTNRDFESKANHLGDTDGTPVKARRHSWRQQIFLRVATPQKACDSPSRYEDYSELGELPPRSPLEPVCEDGPFGPVQEEKKKTSRELRELWKKAILQQILLLRMEKENQKLQASENDLLNKRLKLDYEEITPCLKEVTTVWEKMLSTPGRSKIKFDMEKVHSAVGQGVPRHHRGEIWKFLAEQFHLKHPFPSKQQPKDVPYKELLKKLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLLHMSEEEAFKMLKFLMFDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEYEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLILQHENLETIVDFIKNTLPNLGLVQMEKTISQVFEMDIAKQLQAYEVEYHVLQEELIDSSPLSDNQRMDKLEKTNSSLRKQNLDLLEQLQVANARIQSLEVTVEKLLTSESKLKQAVLTLEMERSALLQMVEELRRQMAQPSTAEPDCTRLEPTGD
Protein: Solute carrier family 11 member 2 (A0A2R8YD71)
Organism: Homo sapiens (Human)
Subcellular location: Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004155}.
Interaction partners:
Sequence:
MVLGPEQKMSDDSVSGDHGESASLGNINPAYSNPSLSQSPGDSEEYFATYFNEKISIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWILLLATLVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVLPRGSTLFLLQVPRVILWLMVELAIIGSDMQEVIGSAIAINLLSVGRIPLWGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLKGMFVPSCSGCRTPQIEQAVGIVGAVIMPHNMYLHSALVKSRQVNRNNKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFGKTNEQVVEVCTNTSSPHAGLFPKDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVVLTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSDFANGLGWRIAGGILVLIICSINMYFVVVYVRDLGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGMSFLDCGHTVSISKGLLTEEATRGYVK
Protein: Suppressor of presenilin protein 4 (O17582)
Organism: Caenorhabditis elegans
Function: Probable transcriptional regulator, which participates in the transcriptional repression of the presenilin protein hop-1. Might play a role in the oxidative stress response.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- REST corepressor spr-1
- Lysine-specific histone demethylase 1
- Suppressor of presenilin-2
- Presenilin sel-12
Sequence:
MSSEPTSSIESDNLRRSKRKKFKLDFVAAAHGNNQKKSRKDPHGQGDDDDDTFDDDLNHFEPLSVLTEQDVSMEMFEDDEEDTVSRRRTRRSTAHFQDYQEPDRWIENSGPHACHKCPSRYESKSSLANHTKMHLGEKRKFACELCDFSASTLKSLTHHNNIHQNFGVLSQQTSPVIPVASSADSTLNSSINSTGCQINAPPAPKLDEEAPIAVESVVVHHEDVAEFDTTPPPILEREDDGPPVLIREAPVRKSNRPMKPTQKAQKMTKQRERKSKTVESPKGSLPSSSASSVTPPPVRKDVEKPKIFVKTTKKNLKKTMKITKVRQRCPHCPFTTSTVTRLNRHSGGHKLKEGYICPSENCNFMCRKAGFLQKHYILHKGTLPWPPEYVKKGGAKMKRTFPESEEKKIEVTEKVQKMKKMHKRRANTVQVVAKAQLKSYIKVEVDDVIFKKCNIGECEFLTQTLTQLIVHKVKTHDTKTAFPQHRFLCLTCGHRAKSYAALRTHKLIEHTSTHKRFHRTYYLKECVGDKFFVKYNLSKVQEEVKEEPKEADGDESGDESFDSMCPASDVHPETLAAIEMKDVFFCCNMCPYKAPTMNRCQRHYDKHFKNDEFKCQYCSWSSRSKEVIVNHEKLHPTVVVANTNEAPVVKNEIEAKVEVLSKTVSSPVECTEESSLSKSIQLWCQREKLRHPELDEQFTRKMIDGVKGFQCTDCPYTSKYRGDMRSHKKRHDIEQLYRCVQCTYTTNRPVSLKDHLKQHAIVNMSIADIKSRRVVVNQGVKIGMRRGVGKDKIYCCDKCPYVTLALGCLWRHHRNHRDTAKINICSNCSYSSIDQRKMEEHTIIHLGLGLNEAVPFVKRVDQKGRPVSSLTDLNSEKMNERKSTKRKMLDKVEKMEVGEDEEDDEESVDKGTDDGDYKQRPEKKRKQSSEEPASDPELFGSSSQPTRQLSERATRNRINYSLLSKNGSGKPTPSTSSANLEKLAGSSGGASSESPEPDESVEVSHWKIRTFLRSEYGVKESLKCPDCPYKSSEPDVLEKHRYYHMTKTTPRPYACSDCTFNTYTPTALLQHLKLHSEGVYFDPMVKKHMKHRKGDSIPPGVKGYYCKNCSFKTSIHRNFIEHSAYHRQQLINRINITLKRQPPRIEYQRPKLKHQFVAKNAKYCKKCTFKCVSQSNFIEHLDRHGWNQLYKCYSCDYSDNTKSVVDFHQLNHHIVKDQTLHSICQSAKFRLENGVIQIPEFQTEKSKPTPDEFVSKTRGLLKCPSCEYFCHVSSELAFHMSVHHLTEPNARETISYLHMGLVPPKATVTTV
Protein: Endoplasmin, putative (Q8I0V4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Endoplasmic reticulum chaperone BIP
- DnaJ protein, putative
- Endoplasmic reticulum chaperone GRP170
- HSP90 co-chaperone p23
- Heat shock protein 70
- Heat shock 70 kDa protein
- Heat shock 70 kDa protein
- HSP40, subfamily A
- Activator of Hsp90 ATPase
- Activator of Hsp90 ATPase, putative
Sequence:
MKLNNIYSFFFLFFVLCVIQENVRRVLCDSSVEGDKGPSDDVSDSSGEKKEVKRDRDTLEEIEEGEKPTESMESHQYQTEVTRLMDIIVNSLYTQKEVFLRELISNAADALEKIRFLSLSDESVLGEEKKLEIRISANKEKNILSITDTGIGMTKVDLINNLGTIAKSGTSNFLEAISKSGGDMSLIGQFGVGFYSAFLVADKVIVYTKNNDDEQYIWESTADAKFTIYKDPRGATLKRGTRISLHLKEDATNLLNDKKLMDLISKYSQFIQFPIYLLHENVYTEEVLADIAKDMVNDPNYDSVKVEETDDPNKKTRTVEKKVKKWTLMNEQRPIWLRSPKELKDEDYKQFFSVLSGYNDQPLYHIHFFAEGEIEFKCLIYIPSKAPSMNDQLYSKQNSLKLYVRRVLVADEFVEFLPRYMSFVKGVVDSDDLPLNVSREQLQQNKILKAVSKRIVRKILDTFHKLYKEGKKNKETLRSELENETDEEKKKEITKKLSEPSTYKLIYKEYRKFLKSGCYEDDINRNKIAKLLLFKTMQYPKSISLDTYIEHMKPDQKFIYYASGDSYEYLAKIPQLQIFKKKNIDVLFLTESVDESCIQRVQEYEGKKFKSIQKGEISFELTEEEKKKEQQMQKMYKALIDVISDTLKNQIFKVEISRRLVDAPCAVVSTEWGLSGQMEKLMKMNVSNSDQIKAMSGQKILEINPNHPIMIDLLKRSVTNPKDLELTNSIKIMYQSAKLASGFDLEDTADLAQIVYDHINQKLGVDNNLKIDDLDPSIFETKKIEDENDSSKFEEEINIDDEIQKKDNNVDNESNDKSDEL
Protein: Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1) (Q7T368)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha
- Pyruvate dehydrogenase E1 component subunit alpha
- Dihydrolipoyl dehydrogenase.
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component subunit alpha
- Transaldolase
- Hi37
- Dihydrolipoamide S-succinyltransferase.
- Pyruvate kinase
Sequence:
MASLRCFLRSGKSAVSAVLRREFHRTPPAAVQVTVRDALNQAMDEELERDERVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPITEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQAVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVLSPWNSEDARGLLKAAIRDDNPVVFLENELMYGVPFEMSEEVQSKDFVIPIGKAKIERQGNHITLVSHSRMVGLCLDAAAVLAKEGIECEVINLRSIRPLDADTIETSITKTNHLVTVEGGWPQFGVGAEILARIMEGPAFNYLDAPAVRVTGVDIPMPYAKILEDNSIPQIKDIIFSVKKTLNV
Protein: Bile acid-sensitive ion channel (BASIC) (Acid-sensing ion channel subunit family member 5) (Amiloride-sensitive cation channel 5) (Brain-liver-intestine amiloride-sensitive Na(+) channel) (BLINaC) (Q9R0W5)
Organism: Rattus norvegicus (Rat)
Function: Cation channel that gives rise to very low constitutive currents in the absence of activation. The activated channel exhibits selectivity for sodium and lithium, and is inhibited by amiloride.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:34549327}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:10457052, ECO:0000269|PubMed:22735174, ECO:0000269|PubMed:27679529}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEHTEKSKGPAEKGLLGKIRRYLSKRPLPSPTDRKKFDHDFAISTSFHGIHNIAQNQNKVRKVIWLSVVLGSVSLLVWQIYSRLVNYFMWPTTTSIEVQYVEKIEFPAVTFCNLNRFQTEAVSRFGIIFFLWDIVSKVLRLQEISGNNTGSPEALDFVASHRNFSITEFVKNNGFYLNHDTLVHCEFFGKTCDPKDFKHVFTEYGNCFTFNYGENVQSKNKVSVSGRGLKLLLDVHQEEFTDNPVPGFADAGVIFVIHSPKKEPQFDGLGLSSPVGMHARVTIRQLKTIHQEYPWGECNPDIKLRNFTTYSTYGCLKECKAKHIQRLCGCLPFLLPGNGVECDLLKYYNCVSPILDHIERKGLCTMGTHNSSCPVPCEETEYPATIAYSTFPSQRATKFLAKKLNQSQEYIRENLVNIEINYSDLNYKITQQQKAVSVPELLADVGGQLGLFCGASLITIIEIIEYLFTSFYWVFIFFLLKILEMIQRTSPPQTV
Protein: Putative protein tag-250 (P34344)
Organism: Caenorhabditis elegans
Interaction partners:
- Splicing factor U2AF 65 kDa subunit
- Branchpoint-bridging protein
Sequence:
MSAVNGLVPSTIFDRINSDMDVSEEMEEIREVLYEMIKTNFPMGVAATHLSEKYHEEFVSKGLGRELPEDWIQQVTAAEEFEAQTRGPITILFVRLSNTSSFKRPPINSVNVRVISTDREPTADELKKIKQRKENEPTEHAKTLSQQSVALKEGSTVSIVYADSPKRFFIRALADDDQYEKIGTTLAEIYAQETPPSALDSRVAIYEIVAGGAYALQDSNGTWFRVIAKQPPQSGQVMCHFVDVGVCEKFPVAAIRLLPPAVHPVMSIGSMAREVRMDVSEEESLRLNNKFVDLTFETKDDGIQVPINLTLSKFDSSDSESLPVVDLQSSDGLSITEFLKKPSGVVRLSTPTKTTSPITPASASTSSLTCLFDKPATIQPMTVAQMPMSAFPANAIFAAGPTDISLRQLSLDPMPDYMYAKLKDECALPDSQLESSPDFGGFYAAFIDDRWERVQCIRASKIDKQAYCVYLLDVGAFQYVRKEAMRRLNSTSPFKKMLMFKCKIGGIKPVAGGEVWSRESHEAVREFFEAACGEPVVVEPTQPGWSQWKQLNAPAVPTCEARLSCCGRDIGDWLIACGLALPINAPIPSPNSQSLLTFVPTPINIVGRNI