wanglab/gogpt-training-data huggingface dataset:
Protein: Guanylyl cyclase-activating protein 2 (GCAP 2) (Guanylate cyclase activator 1B) (Q9UMX6)
Organism: Homo sapiens (Human)
Function: Stimulates two retinal guanylyl cyclases (GCs) GUCY2D and GUCY2F when free calcium ions concentration is low, and inhibits GUCY2D and GUCY2F when free calcium ions concentration is elevated (By similarity). This Ca(2+)-sensitive regulation of GCs is a key event in recovery of the dark state of rod photoreceptors following light exposure (By similarity). May be involved in cone photoreceptor response and recovery of response in bright light (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P51177}; Lipid-anchor {ECO:0000250|UniProtKB:P51177}. Photoreceptor inner segment {ECO:0000269|PubMed:9620085}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:9620085}. Note=Subcellular location is not affected by light or dark conditions. {ECO:0000250|UniProtKB:Q8VBV8}.
Interaction partners:
- Retinal guanylyl cyclase 1
- Retinal guanylyl cyclase 2
- Guanylyl cyclase-activating protein 1
- Guanylyl cyclase-activating protein 3
- Photoreceptor disk component PRCD
- Cyclic nucleotide-gated channel alpha-1
- Cyclic nucleotide-gated channel beta-1
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Tyrosine-protein kinase Mer
- Tubby-related protein 1
Sequence:
MGQEFSWEEAEAAGEIDVAELQEWYKKFVMECPSGTLFMHEFKRFFKVTDDEEASQYVEGMFRAFDKNGDNTIDFLEYVAALNLVLRGTLEHKLKWTFKIYDKDGNGCIDRLELLNIVEGIYQLKKACRRELQTEQGQLLTPEEVVDRIFLLVDENGDGQLSLNEFVEGARRDKWVMKMLQMDMNPSSWLAQQRRKSAMF
Protein: Atrial natriuretic peptide receptor 3 (Atrial natriuretic peptide clearance receptor) (Atrial natriuretic peptide receptor type C) (ANP-C) (ANPR-C) (NPR-C) (P17342)
Organism: Homo sapiens (Human)
Function: Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May regulate diuresis, blood pressure and skeletal development. Does not have guanylate cyclase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30032985}; Single-pass type I membrane protein.
Interaction partners:
- Natriuretic peptides A
- Natriuretic peptides B
- C-type natriuretic peptide
- Guanylate cyclase activator 2B
- Guanylin
- Neuronal pentraxin receptor
- Guanylyl cyclase C
- Emerin
- Na
- Osteocrin
Sequence:
MPSLLVLTFSPCVLLGWALLAGGTGGGGVGGGGGGAGIGGGRQEREALPPQKIEVLVLLPQDDSYLFSLTRVRPAIEYALRSVEGNGTGRRLLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARGAKPDLILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDSEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEDIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTSGDYAFFNIELFNSSSYGDGSWKRGDKHDFEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNMEDYVNMFVEGFHDAILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVIAMTDVEAGTQEVIGDYFGKEGRFEMRPNVKYPWGPLKLRIDENRIVEHTNSSPCKSSGGLEESAVTGIVVGALLGAGLLMAFYFFRKKYRITIERRTQQEESNLGKHRELREDSIRSHFSVA
Protein: Proline-rich membrane anchor 1 (PRiMA) (Q810F0)
Organism: Mus musculus (Mouse)
Function: Required to anchor acetylcholinesterase (ACHE) to the basal lamina of the neuromuscular junction and to the membrane of neuronal synapses in brain. Also able to organize ACHE into tetramers.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Cell junction. Synapse. Note=In the brain, PRIMA linked to ACHE is found in membrane rafts.
Interaction partners:
- Acetylcholinesterase collagenic tail peptide
- Cellular tumor antigen p53
Sequence:
MLLRDLVPRHGCCWPSLLLHCALHPLWGLVQVTHAEPQKSCSKVTDSCQHICQCRPPPPLPPPPPPPPPPRLLSAPAPNSTSCPAEDSWWSGLVIIVAVVCASLVFLTVLVIICYKAIKRKPLRKDENGTSVAEYPMSSSQSHKGVDVNAAVV
Protein: BAR/IMD domain-containing adapter protein 2-like 2 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2) (BAI1-associated protein 2-like protein 2) (Planar intestinal- and kidney-specific BAR domain protein) (Pinkbar) (Q6UXY1)
Organism: Homo sapiens (Human)
Function: Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21743456}; Peripheral membrane protein {ECO:0000269|PubMed:21743456}. Cell junction {ECO:0000269|PubMed:21743456}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21743456}. Note=Localizes to RAB13-positive vesicles and to the plasma membrane at intercellular contacts.
Interaction partners:
- Dol-P-Man:Man
- Dol-P-Man:Man
- Potassium voltage-gated channel subfamily KQT member 5
- AP-2 complex subunit sigma
- Aftiphilin
- SH3-containing GRB2-like protein 3-interacting protein 1
- Clathrin light chain B
- AP-1 complex subunit sigma-1A
- AP-2 complex subunit alpha-1
- Phosphatidylinositol-binding clathrin assembly protein
Sequence:
MAPEMDQFYRSTMAIYKSIMEQFNPALENLVYLGNNYLRAFHALSEAAEVYFSAIQKIGERALQSPTSQILGEILVQMSDTQRHLNSDLEVVVQTFHGGLLQHMEKNTKLDMQFIKDSRQHYELEYRHRAANLEKCMSELWRMERKRDKNVREMKESVNRLHAQMQAFVSESQRAAELEEKRRYRFLAEKHLLLSNTFLQFFGRARGMLQNRVLLWKEQSEASRSPSRAHSPGLLGPALGPPYPSGRLTPTCLDMPPRPLGEFSSPRSRHGSGSYGTEPDARPASQLEPDRRSLPRTPSASSLYSGSAQSSRSNSFGERPGGGGGARRVRALVSHSEGANHTLLRFSAGDVVEVLVPEAQNGWLYGKLEGSSASGWFPEAYVKALEEGPVNPMTPVTPMTSMTSMSPMTPMNPGNELPSRSYPLRGSHSLDDLLDRPGNSIAPSEYWDGQSRSRTPSRVPSRAPSPAPPPLPSSRRSSMGSTAVATDVKKLMSSEQYPPQELFPRGTNPFATVKLRPTITNDRSAPLIR
Protein: Protein sprouty homolog 1 (B5DFH3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- Growth factor receptor-bound protein 2
- E3 ubiquitin-protein ligase CBL
- SOS Ras/Rac guanine nucleotide exchange factor 1
- SOS Ras/Rho guanine nucleotide exchange factor 2
- Receptor protein-tyrosine kinase
Sequence:
MDSPSQHDSHTSLVVIQPPAVEGRQRLDYDRDTQPATILSLDQIKAIRGSNEYTEGPSVARRPAPRTAPRPEKQERTHEIIPANVNSSYVHRPAGHSGNARGSVLSRSTSTGSAASSGSSSSVSSEQGLLGRSPPTRPIPGHRSDRVIRTQPKQLLVDDLKASLKEDPTQHKFICEQCGKCKCGECTAPRALPSCLACDRQCLCSAESMVEYGTCMCLVKGIFYHCSNDDDGGSYSDNPCSCSQSHCCSRYLCMGALSLCLPCLLCYPPAKGCLKLCRGCYDWTHRPGCRCRNSNTVYCKLESCPSRAQGKPS
Protein: Phosphate transporter (Q9VTG0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363058}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363058}.
Interaction partners:
Sequence:
MESFAPELLWMVVIGFLIAFVLAFGIGANDVANSFGTSVGSGVLTIRQACVLATICEISGAVLIGYKVSDTMRKGILEVGLYEGAEEVLMLGCVAALASSAVWLLVATFLKLPISGTHSIVGSTIGFSLVARGVQGLKWSTLGTIVGSWFISPVLSGIVSILLFLAIRRFILRAQEPLKAGFRSLPIFYGVTFFINVISVVLDGPKLLYMDNIPTWIALTASFGLSLLVALLTQLVVVPLQRRKIAKRLRAENPVKFNFEDSVESSPSGSPKKQRRPLSLVSEGKPLPAIAEITELVSLSDNSPRTFKLAPFGLAAKNNNALGEEYKIDPQLIKKAEDLLGKASLDNTDLTITSLNFIDEQQQQQQQQQNGRKLQECFKRMQSPKEEQKSKTNSIGTDLETGSTKATNNNLQVVESGGSLDLMISSTLSPNSSKVPLIESKEALNEQEEELKRTTGGGRRTSGAEETPEISMLFSFLQILTATFGSFAHGGNDVSNAIGPLIALYMIYREGSVMQQAESPIYILIYGGIGISVGLWLWGRRVIETIGNDLTKITSSTGFTIEVGAAITVLLASKIGLPISTTHCKVGSVVFVGHVSASGRKKKSQPNDQTDKETHNEVAPMDDGSVDWHLFRNIAYAWIVTVPVTALLSAGMMYVLCAIAVDDMGGA
Protein: Disintegrin and metalloproteinase domain-containing protein 29 (ADAM 29) (Cancer/testis antigen 73) (CT73) (Q9UKF5)
Organism: Homo sapiens (Human)
Function: May be involved in spermatogenesis and fertilization. Seems to be a non catalytic metalloprotease-like protein.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MKMLLLLHCLGVFLSCSGHIQDEHPQYHSPPDVVIPVRITGTTRGMTPPGWLSYILPFGGQKHIIHIKVKKLLFSKHLPVFTYTDQGAILEDQPFVQNNCYYHGYVEGDPESLVSLSTCFGGFQGILQINDFAYEIKPLAFSTTFEHLVYKMDSEEKQFSTMRSGFMQNEITCRMEFEEIDNSTQKQSSYVGWWIHFRIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLIVVDDVRKSVHLYCKWKSENITPRMQHDTSHLFTTLGLRGLSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDTCRCSQPRCIMHEGNPPITKFSNCSYGDFWEYTVERTKCLLETVHTKDIFNVKRCGNGVVEEGEECDCGPLKHCAKDPCCLSNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDDFYVEDGIPCKERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTEIPNMSDHTTVHWARFNDIMCWSTDYHLGMKGPDIGEVKDGTECGIDHICIHRHCVHITILNSNCSPAFCNKRGICNNKHHCHCNYLWDPPNCLIKGYGGSVDSGPPPKRKKKKKFCYLCILLLIVLFILLCCLYRLCKKSKPIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPPVTPS
Protein: Epididymis secretory sperm binding protein (A0A384MEK2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCSAFHRAESGTELLARLEGRSSLKEIEPNLFADEDSPVHGDILEFHGPEGTGKTEMLYHLTARCILPKSEGGLEVEVLFIDTDYHFDMLRLVTILEHRLSQSSEEIIKYCLGRFFLVYCSSSTHLLLTLYSLESMFCSHPSLCLLILDSLSAFYWIDRVNGGESVNLQESTLRKCSQCLEKLVNDYRLVLFATTQTIMQKASSSSEEPSHASRRLCDVDIDYRPYLCKAWQQLVKHRMFFSKQDDSQSSNQFSLVSRCLKSNSLKKHFFIIGESGVEFC
Protein: Endoribonuclease Dicer homolog 3 (EC 3.1.26.-) (Dicer-like protein 3) (AtDCL3) (Q9LXW7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ribonuclease (RNase) III involved in RNA-mediated post-transcriptional gene silencing (PTGS). Involved in the processing of repeat-associated small interfering RNAs (ra-siRNAs, derived from heterochromatin and DNA repeats such as transposons) by cleaving small dsRNAs into 24 nucleotide ra-siRNAs. Plays a role in antiviral RNA silencing. Involved in the production of viral siRNAs derived from the cabbage leaf curl virus (CaLCuV) and tobacco rattle virus (TRV). Targeted by the viral silencing suppressor (VSR) protein 2b of the cucumber mosaic virus (CMV) that inactivates DCL3 function in RNA silencing. Acts redundantly with DICER-LIKE 1 (DCL1) to promote flowering via repression of FLOWERING LOCUS C (FLC). Does not seem to be involved in microRNAs (miRNAs) processing.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15024409, ECO:0000269|PubMed:16839878}.
Interaction partners:
- Protein argonaute 4
- RNA-dependent RNA polymerase 2
- Protein argonaute 6
- Double-stranded RNA-binding protein 3
- RNA-dependent RNA polymerase 6
- Protein argonaute 1
- Protein argonaute 2
- Protein argonaute 9
- Protein DCL homolog, chloroplastic
- Protein argonaute 7
Sequence:
MHSSLEPEKMEEGGGSNSLKRKFSEIDGDQNLDSVSSPMMTDSNGSYELKVYEVAKNRNIIAVLGTGIDKSEITKRLIKAMGSSDTDKRLIIFLAPTVNLVKQQCCEIRALVNLKVEEYFGAKGVDKWTSQRWDEEFSKHDVLVMTPQILLDVLRSAFLKLEMVCLLIIDECHHTTGNHPYAKLMKEFYHESTSKPKIFGLTASAVIRKGIVSSPSNYAAQVSELERLMDSKIFNPEEREGVEKFATTVKEGPILYNPSPSCSLELKEKLETSHLKFDASLRRLQELGKDSFLNMDNKFETYQKRLSIDYREILHCLDNLGLICAHLAAEVCLEKISDTKEESETYKECSMVCKEFLEDILSTIGVYLPQDDKSLVDLQQNHLSAVISGHVSPKLKELFHLLDSFRGDKQKQCLILVERIITAKVIERFVKKEASLAYLNVLYLTENNPSTNVSAQKMQIEIPDLFQHGKVNLLFITDVVEEGFQVPDCSCMVCFDLPKTMCSYSQSQKHAKQSNSKSIMFLERGNPKQRDHLHDLMRREVLIQDPEAPNLKSCPPPVKNGHGVKEIGSMVIPDSNITVSEEAASTQTMSDPPSRNEQLPPCKKLRLDNNLLQSNGKEKVASSKSKSSSSAAGSKKRKELHGTTCANALSGTWGENIDGATFQAYKFDFCCNISGEVYSSFSLLLESTLAEDVGKVEMDLYLVRKLVKASVSPCGQIRLSQEELVKAKYFQQFFFNGMFGKLFVGSKSQGTKREFLLQTDTSSLWHPAFMFLLLPVETNDLASSATIDWSAINSCASIVEFLKKNSLLDLRDSDGNQCNTSSGQEVLLDDKMEETNLIHFANASSDKNSLEELVVIAIHTGRIYSIVEAVSDSSAMSPFEVDASSGYATYAEYFNKKYGIVLAHPNQPLMKLKQSHHAHNLLVDFNEEMVVKTEPKAGNVRKRKPNIHAHLPPELLARIDVPRAVLKSIYLLPSVMHRLESLMLASQLREEIDCSIDNFSISSTSILEAVTTLTCPESFSMERLELLGDSVLKYVASCHLFLKYPDKDEGQLSRQRQSIISNSNLHRLTTSRKLQGYIRNGAFEPRRWTAPGQFSLFPVPCKCGIDTREVPLDPKFFTENMTIKIGKSCDMGHRWVVSKSVSDCAEALIGAYYVSGGLSASLHMMKWLGIDVDFDPNLVVEAINRVSLRCYIPKEDELIELERKIQHEFSAKFLLKEAITHSSLRESYSYERLEFLGDSVLDFLITRHLFNTYEQTGPGEMTDLRSACVNNENFAQVAVKNNLHTHLQRCATVLETQINDYLMSFQKPDETGRSIPSIQGPKALGDVVESIAGALLIDTRLDLDQVWRVFEPLLSPLVTPDKLQLPPYRELNELCDSLGYFFRVKCSNDGVKAQATIQLQLDDVLLTGDGSEQTNKLALGKAASHLLTQLEKRNISRKTSLGDNQSSMDVNLACNHSDRETLTSETTEIQSIVIPFIGPINMKKGGPRGTLHEFCKKHLWPMPTFDTSEEKSRTPFEFIDGGEKRTSFSSFTSTITLRIPNREAVMYAGEARPDKKSSFDSAVVELLYELERRKIVIIQK
Protein: Rifin (Q8IAS6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MRIHYINMFLFSLMFNILLNVNKNHYNTTLHTPNTTKIPTTRLLCECELYAPSNYNNDPEMKQVMDNFDRHTQQRFHEYEQRMIKNRKECKEQCEQNIQKLILKEKIQKELKEKFSALQIDISTHDIPTCVCEKSVADKTEKFCLKCGYGLGGALTAWQIFGYTGIYGWANYAALLAHEAGVKAGIKVVIDMFSTYPGLISLPGVDLTKMINGSNFNIPMELVNIVKGLSNGLCKTPNKHLFCAFTNMEKGQSLVSFANSASQSGIMEAASVQGAKVAIIKTTTADFSYNMIVSGITIFVIVLVMVIIYFILRYRRKKKMKKKLQYIKLLKE
Protein: Kinase suppressor of Ras 2 (hKSR2) (EC 2.7.11.1) (Q6VAB6)
Organism: Homo sapiens (Human)
Function: Location-regulated scaffold connecting MEK to RAF. Has very low protein kinase activity and can phosphorylate MAP2K1 at several Ser and Thr residues with very low efficiency (in vitro). Acts as MAP2K1/MEK1-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1. Interaction with BRAF enhances KSR2-mediated phosphorylation of MAP2K1 (in vitro). Blocks MAP3K8 kinase activity and MAP3K8-mediated signaling. Acts as a negative regulator of MAP3K3-mediated activation of ERK, JNK and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8 production.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 1
- Kinase suppressor of Ras 1
- BRCA1-associated protein
- Serine/threonine-protein kinase B-raf
- Dual specificity mitogen-activated protein kinase kinase 2
- Mitogen-activated protein kinase 3
Sequence:
MDEENMTKSEEQQPLSLQKALQQCELVQNMIDLSISNLEGLRTKCATSNDLTQKEIRTLESKLVKYFSRQLSCKKKVALQERNAELDGFPQLRHWFRIVDVRKEVLEEISPGQLSLEDLLEMTDEQVCETVEKYGANREECARLNASLSCLRNVHMSGGNLSKQDWTIQWPTTETGKENNPVCPPEPTPWIRTHLSQSPRVPSKCVQHYCHTSPTPGAPVYTHVDRLTVDAYPGLCPPPPLESGHRSLPPSPRQRHAVRTPPRTPNIVTTVTPPGTPPMRKKNKLKPPGTPPPSSRKLIHLIPGFTALHRSKSHEFQLGHRVDEAHTPKAKKKSKPLNLKIHSSVGSCENIPSQQRSPLLSERSLRSFFVGHAPFLPSTPPVHTEANFSANTLSVPRWSPQIPRRDLGNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRGDPARLVRTESVPCDINNPLRKPPRYSDLHISQTLPKTNKINKDHIPVPYQPDSSSNPSSTTSSTPSSPAPPLPPSATPPSPLHPSPQCTRQQKNFNLPASHYYKYKQQFIFPDVVPVPETPTRAPQVILHPVTSNPILEGNPLLQIEVEPTSENEEVHDEAEESEDDFEEMNLSLLSARSFPRKASQTSIFLQEWDIPFEQLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQAGRREDKLRIQNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKLPKRNRRLSHPGHFWKSAEL
Protein: Transcriptional regulator ERG (Transforming protein ERG) (P11308)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Interaction partners:
- Transmembrane protease serine 2
- Androgen receptor
- Runt-related transcription factor 2
- Histone-lysine N-methyltransferase SETDB1
- Core-binding factor subunit beta
- Serine/arginine-rich splicing factor 10
- RNA-binding protein EWS
- Voltage-gated inwardly rectifying potassium channel KCNH6
- Speckle-type POZ protein
Sequence:
MASTIKEALSVVSEDQSLFECAYGTPHLAKTEMTASSSSDYGQTSKMSPRVPQQDWLSQPPARVTIKMECNPSQVNGSRNSPDECSVAKGGKMVGSPDTVGMNYGSYMEEKHMPPPNMTTNERRVIVPADPTLWSTDHVRQWLEWAVKEYGLPDVNILLFQNIDGKELCKMTKDDFQRLTPSYNADILLSHLHYLRETPLPHLTSDDVDKALQNSPRLMHARNTGGAAFIFPNTSVYPEATQRITTRPDLPYEPPRRSAWTGHGHPTPQSKAAQPSPSTVPKTEDQRPQLDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSSNSSCITWEGTNGEFKMTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQPHPPESSLYKYPSDLPYMGSYHAHPQKMNFVAPHPPALPVTSSSFFAAPNPYWNSPTGGIYPNTRLPTSHMPSHLGTYY
Protein: Phosphoglycerate mutase 1 (PGAM 1) (EC 5.4.2.11) (BPG-dependent PGAM 1) (MPGM 1) (Phosphoglyceromutase 1) (P00950)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyzes the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Mitochondrion outer membrane {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:16962558}; Peripheral membrane protein {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:16962558}; Cytoplasmic side {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:16962558}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Interaction partners:
- Fructose-bisphosphate aldolase
- Phosphoglycerate mutase 2
- Phosphoglycerate mutase 3
- Phosphoglycerate kinase
- Enolase 2
- Enolase 1
- Triosephosphate isomerase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Pyruvate kinase 1
Sequence:
MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK
Protein: Gastric triacylglycerol lipase (GL) (Gastric lipase) (EC 3.1.1.3) (Lingual lipase) (P04634)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol. Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P80035}.
Interaction partners:
- Pancreatic triacylglycerol lipase
- Bile salt-activated lipase
- Pancreatic lipase-related protein 2
- Inactive pancreatic lipase-related protein 1
- Endothelial lipase
- Hepatic triacylglycerol lipase
- Diacylglycerol O-acyltransferase 1
- Lipoprotein lipase
- Acylglycerol transacylase
- Patatin-like phospholipase domain-containing protein 2
Sequence:
MWLLLITSVISTFGGAHGLFGKLGPGNPEANMNISQMITYWGYPCQEYEVVTEDGYILGVYRIPHGKNNSENIGKRPVVYLQHGLIASATNWIANLPNNSLAFMLADAGYDVWLGNSRGNTWSRKNVYYSPDSVEFWAFSFDEMAKYDLPATINFIVQKTGQEKIHYVGHSQGTTIGFIAFSTNPTLAKKIKTFYALAPVATVKYTQSPLKKISFIPTFLFKLMFGKKMFLPHTYFDDFLGTEVCSREVLDLLCSNTLFIFCGFDKKNLNVSRFDVYLGHNPAGTSVQDFLHWAQLVRSGKFQAFNWGSPSQNMLHYNQKTPPEYDVSAMTVPVAVWNGGNDILADPQDVAMLLPKLSNLLFHKEILAYNHLDFIWAMDAPQEVYNEMISMMAED
Protein: Mite allergen Der p 5 (Allergen Der p V) (IgE-binding allergen) (allergen Der p 5) (P14004)
Organism: Dermatophagoides pteronyssinus (European house dust mite)
Interaction partners:
Sequence:
MKFIIAFFVATLAVMTVSGEDKKHDYQNEFDFLLMERIHEQIKKGELALFYLQEQINHFEEKPTKEMKDKIVAEMDTIIAMIDGVRGVLDRLMQRKDLDIFEQYNLEMAKKSGDILERDLKKEEARVKKIEV
Protein: RE45537p (Tondu-domain-containing growth inhibitor, isoform B) (Q8IQJ9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METALDVLSRAATMVQNNPSEMRATSKVLTTTKWRRERRQRSAGYQPHEAGNSERERERERDREDRDMDSPIDMSVTTGALKQRASPPPPYREPLPGTNYAANSRPSVITQAPPKREPPEQAHSTDMAMCDIDEHFRRSLGENYAALFAKKSPTPTPTPTPSPSGTPKQQVSPLAYGLPSSTSTAASQHYQQQRSPLAKSGWVILEPESLQPELPPPQEEPLPLSLALHRTQTPPSPPPSATGSAPALPTAVSQVMEAAVAGRRILDTPHHTPPRYNTPPPPPPAYGIAGTTVVAPTLTPTPTPNPTPSQIPTPTPSMPAIIRVKAEPGLAAVAASSTQTPPASPTSSTNISIFTKTEASVDDHFAKALGETWKKLQGGHKE
Protein: Large ribosomal subunit protein uL1c (50S ribosomal protein L1, chloroplastic) (CL1) (Q9LY66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein binds directly to 23S ribosomal RNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein uL3c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein bL28c
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Large ribosomal subunit protein bL31c
- Large ribosomal subunit protein bL21c
- Large ribosomal subunit protein uL13c
Sequence:
MAACATHSSLMLAYAAASTRSQDLTPTPSLFSFASSRPNHLSFPLLLLGGSRDRRCAAIDRASNHKFIVSAVAAEADLDTEEDLEQTATAVLDPPKPKKGKAALVLKRDRTRSKRFLEIQKLRETKKEYDVNTAISLLKQTANTRFVESVEAHFRLNIDPKYNDQQLRATVSLPKGTGQTVIVAVLAQGEKVDEAKSAGADIVGSDDLIEQIKGGFMEFDKLIASPDMMVKVAGLGKILGPRGLMPNPKAGTVTANIPQAIEEFKKGKVEFRADKTGIVHIPFGKVNFTEEDLLINFLAAVKSVETNKPKGAKGVYWKSAHICSSMGPSIKLNIREMIDFKPPTAN
Protein: Vitellogenin receptor (SiVgR) (Q6X0I2)
Organism: Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri)
Function: Involved in uptake of vitellogenin by endocytosis. Expression is regulated by the juvenile hormone analog, methoprene (in vitro).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRFIVLLFICSFIYPCYVSSIGFRRISKVSLKKTKCEDGYFQCNSGECIPVDKKCDYIDHCIDGSDEDFECDHLDEKSFITCAKDQFKCKNQECIPAAKYCDMVNDCLDESDEHDGCVKHLNCTNKFLCTDGHCINKEWVCDGRNDCPDGNDEWNCKANKTSSASSCKTENYQYMCANHRCISLKVVCDKKDDCGDGSDEGPGCTQFNCSSAGCQSNCHQTPKGSVCTCKPGYKLQKDNRTCNDIDECQAYGICDQDCMNVPGSYACTCQREYYLENDKRTCKARAGEATLVFSTRTSILGMHVDSEKFFSLATNLNHAVGVAMYGDYVYWSNLEENGYNTIVKKRTYHPQAPNEVIVTTGLALITGIDVDWITKNIYFADEDNHCIGVCTNDGTYCTVLIKDTDKPTGVALLPTQGKMYWSDWGTFPHIAVAGMDGKNVRIFVNVKLEWPKSVTIDYPNERLYWVDAKSKMIESVRLDGTDRRIVLHDIIQEPFSMTVFQNKLYWSDWESNGIQTCNKFTGKDWKILIRNHNKPYSVHMDHSAIKPNIDNPCYSNPCSQLCMLNQNKGYTCGCTLDKKLNADKHTCQDVKKNQHLLIIQGRKFINYYHEFLGKPKVMTLSLQHMSQQSYNNLVNIISDPLSGQIIICHLQLSTPFLTSTTDILRYDPVHHSSEKIVTINKIFFELAFDYIGNNLYTTNTVNQSIEVINLNTKAMTAFYFKDEVPKYIALAPEESKMFVAFQKSMHSISGLTLYEMQMNGLGKRKLIREGLIGPQLPMYYDRDSKTLFVSDLLPGYIYSHSAQDTRILRSGLKSPHSLTVAGDNLFWIESQNKLYSTNFRTASVKQKTVEFDLSKLNDNMTSLPGHLTPYSRDAQYVVTLRKDDIPKHDCQKNNGNCSHVCLPSLITSFICACPPGMELSNDNRTCISHHECSKNEYKCSEHNICIQRNQLCDGIENCPNGEDETSECRIKGRCKENQFMCKNGDCIRLKDRCNSRYDCTDQSDEQNCEKPKCKSDEFQCKFTETCIPKTKMCDSNPDCDDLSDEEDCRKVECTSNEFKCNNGKCIPNTFVCDNDNDCEDGEDEAAEKCYSKIACKMPKMFKCPNGDCISDSLLCNGINDCNDGSDEVHCLSNVTTHLVNCSLNEYRCLGTDICLPKNVRCDGKNDCPQSDDEQNCTYCFENEFACDNKRCIPELWVCDKANDCGDNSDEKNCDGSKRNFIESNECDEFKCSVGTCLPYSKVCDGNRDCPDGSDETGKCQTACTVNNFCKGMCYKTPAGAVCGCQSGYRLAVDMISCEDINECELDICSQMCRNTIGSYECFCKDEFIIRNDKTSCKAVGPAMEFITVTDNDIRKMTHNLHSTTQLLFPLMGVRVSGLDVNAVSDSVYWSNDEFGTIKKLNIRTNEIVTVKIVEHPQALAVDWITGNVYVNDNSHLNTIKVCNLEKGKCATLVKIQDKMKVASVIVDSINRWLFWAEISLEADHPTSKICRTDMTGADMKIIASDLGFVRGMTIDHVKSKLYWSDDFYKTVESSNFDGSQRKVVLTLNMNHALSISIFEQSLYFLSSDNLLSSCKMYGKRSCEHVNIGANNVFRLFSILHISRQVPFANPCDAEYCDYMCVLKKENATCICSDGESIESNSTCNIKNDLKFVESINFSRNTRNISGIYSITIIVLLVSVLLLCVYYYYQKNKLKSKPASNLSCSSIHFQNPSYDRSDEIEVMLDSMASSELSPGQHEYINPINNKGMKAAENNAKKSNQCSEGKNIEEEKQDALIYFVHNSK