wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar protein sorting-associated protein 28 (ESCRT-I complex subunit VPS28) (Q02767)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for normal endocytic and biosynthetic traffic to the yeast vacuole.
Subcellular location: Cytoplasm. Endosome. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 25
- Vacuolar-sorting protein SNF7
- Vacuolar-sorting protein SNF8
- Multivesicular body sorting factor 12
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein-sorting-associated protein 24
- Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
- Protein SRN2
- Vacuolar protein-sorting-associated protein 36
- DOA4-independent degradation protein 4
Sequence:
MQKHNIKLNQNQDISQLFHDEVPLFDNSITSKDKEVIETLSEIYSIVITLDHVEKAYLKDSIDDTQYTNTVDKLLKQFKVYLNSQNKEEINKHFQSIEAFCDTYNITASNAITRLERGIPITAEHAISTTTSAPSGDNKQSSSSDKKFNAKYVAEATGNFITVMDALKLNYNAKDQLHPLLAELLISINRVTRDDFENRSKLIDWIVRINKLSIGDTLTETQIRELLFDLELAYKSFYALLD
Protein: Glutathione S transferase E12, isoform A (Glutathione S transferase E12, isoform B) (Glutathione S transferase E12, isoform C (EC 2.5.1.18)) (Glutathione S transferase E12, isoform D) (Q9XYZ9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH16740p
- Bifunctional glutamate/proline--tRNA ligase
- Glutathione S-transferase S1
- Myc proto-oncogene protein
- Glutathione S transferase O1
- Glutathione S transferase O3
- Glutathione S-transferase D1
- Pyrimidodiazepine synthase
- Glutathione peroxidase
- glutathione transferase
Sequence:
MSKPALYYATLSPPSRAVLLTAKAIGLDLELRPINLLKGEHLTPEFLKLNPQHTIPTLIDGEATIIDSHAICAYLVEKYGQKEQQLYPKELVQRANVDARLHLDSGHLFARLRFLYEPILYYGSTDCSIDKIAYIQKCWEILEGFLKDQPYLCGSDLTIADFCAVATVTSVNDTAPIDEFKFPKMHAWLKRLAELPYYQEVNGDGADELKSIFKAKLAENRGK
Protein: Zinc finger protein 330 (Nucleolar autoantigen 36) (D6R8Y9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MPKKKTGARKKAENRREREKQLRASRSTIDLAKHPCNASMECDKCQRRQKNRAFCYFCNSVQKLPICAQCGKTKCMMKSSDCVIKHAGVYSTGLAMVGAICDFCEAWVCHGRKCLSTHACACPLTDAECVECERGVWDHGGRIFSCSFCHNFL
Protein: Vacuolar protein sorting-associated protein 4B (EC 3.6.4.6) (Suppressor of K(+) transport growth defect 1) (Protein SKD1) (P46467)
Organism: Mus musculus (Mouse)
Function: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:12594041}; Peripheral membrane protein {ECO:0000305}. Note=Membrane-associated in the prevacuolar endosomal compartment.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1 homolog
- Charged multivesicular body protein 5
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 1B1
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 6
- Charged multivesicular body protein 2b
- Vacuolar protein sorting-associated protein 4A
- IST1 homolog
- Charged multivesicular body protein 1B2
Sequence:
MASTNTNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCTEYLDRAEKLKEYLKKKEKKPQKPVKEEQSGPVDEKGNDSDGEAESDDPEKKKLQNQLQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPLPEAHARAAMFRLHLGSTQNSLTEADFQELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVRGPSRADPNCIVNDLLTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMWDMLRSLSSTKPTVNEQDLLKLKKFTEDFGQEG
Protein: Syndecan-binding protein (syntenin) (Syntenin-1) (F1QFG9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Tetraspanin
- Tetraspanin
Sequence:
MSLYPSLEDMKVDKFIQAHNTPTASPSKALPLPEPSSDQNEPSTYYDSKAEQTGTSSRLYPELNEFMGLNLSSDALQTFSSSIADQTAGALSVCTSGMSWAAAPITGSDLGVKRAEIRQGVREVVLCKDMDGKIGLRLKAIDNGVFVQLVQANTAAALAGLRFGDQILEINGKSCAGWNSDYAHKVLKNSNPERITLAVRDRPLERTVTLHKDMNGQLGFIFRKGRITSIVKDSSSARNGLLTDHQICEINGQNIIGLKDTQIMDILNSSGGVVTITVMPVVIFEHMMKRMSSSIVKSLMDHSIPEV
Protein: Circadian clock-controlled protein daywake (O76879)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the circadian clock or downstream effector of clock function. Required for suppressing daytime sleep (siesta) under ambient environmental temperatures. Part of a heat avoidance mechanism that modulates daytime sleep behavior under different environmental temperatures to minimize the risk of heat exposure. Under cooler ambient temperatures, suppresses daytime sleep (siesta) and thus allows for longer periods of daytime activity.
Interaction partners:
- RH37844p
Sequence:
MQLTGASMFLVWVGLLSWVSCRVDASEGFPSPLKRCKLQDESCLLAQAQTFFQAFKNGIPERQVAALEPIALGTMFIESGGHSESIKFKLTMSDAKLYNLANSMMVKSLKGFTKDLTRPLKLTLLLDNPELEVRAKYDVDGKLLILPIVSKGDLTIRLNDVHTKVWITAEPVKRSDGHTYLNITDYKTATKIKGGHFDLSNLFNDNKELRDSTLKVLNQEWSTLALDVQPKINEACAKAFSAIVQSLWANIPYDEFFEKE
Protein: Kinesin, putative (Q57XU6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGKSEGIRVFLRIRPAAKGLPRPLNGVGSVRGADDTQNYSVEHTFEHSTVRFHVDRRTDADVVNNTREDFTFTFRRAFEPNATQADVFNTVAKDCVLAALDGYNSTVFAYGQTGSGKTHSITGGAESYEDRGIIPRALALLYEEIARRQQQEGTYSVAISYLQIYNDKGQDLLNRGHDARKLEDLPVVTIHDGGSDSDEVALRGLAQHSAATPKDALNLLFLGDTNRLYCETPMNKTSSRSHCVFTIYLEARPHGASVVRRSKLHFVDLAGSERVAKTGVSGTVLTEAKYINLSLHYLEQVIMALSEQANGRREHVPFRNSFMTMVLRDSLGPNCKTSMLATAHPAVDQLPETISTCRFAQRVALIKQDAHVNEEVDPHVLVRKLKAELQQMRDRLAFYTKDGGGAPDRDLSDDEKLRCEEMVKRFIAATDGNAKLEGFDGDLARIYYCFDVLKRMLAEGGAGVRVGGCGAGSSGGLSEQQQQQLDMYRSRVDALELCVKQKENEMNMLFDALQKVHRAKYNAETQTGADDGESSNYASRTKTAPGTGGSVEGGHAAPFQKPLGHPSNGAHMYASAAAAQQPHGMNVVEAGHSSNAGSIRYDGQDSPQALRRMACERLAPAEVTAVDEFFEKQQQLNEVYDLSSLTDAELLQDRATAFEAFSRSYRQCAQMESNKQELKARYETCKTTARQLNEVVDQIRKLKGCIQRLRAERVLQGVEEVDEAERNALEELAAHKTSYNDLAASLRQQKESIDAMHLFMKRAQEQLTKDFEDWLQIRQKQLIMAVKAGGYKNADSSGSSNGVSIASNTTTMSNNIATPQVNPTTTAAVTTATIPPPTEKAPPTAAAASPGRPTCFKPRLNFLQEQMQSKQQLGEQKPASASMPDLPPLREGLSSRRSWGCDGGMQLRGGLLHTGGLGSAPTHTRASSDTECGRLHHSVPATLSQQSTPNNRLGQPSTMVPLGGSALRNGWTGGSSSGAINDNNGNGYGVTSGISAGGAGLDAPNPYAPEYRSTGDPAADKQLAELYKARDALRLQLDPPQ
Protein: Rifin (Q8I4N9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYTNILLFPLKLNILVNTHKKPSITPRHIQTTRLLCECELYMSNYDNDPEMKRVMQQFHDRTTQRFHEYDDRMIEKRQKCKDRCNKEIEKIILKDKIEKELTETFATLNTNITNEDIPTCICKKSVADKIEKTCLKYGGALGGGVMPGLGLIGGNSVYILANYETINAFIAKTIEELEGIPGITKLFGAKISQFVTPAVFRKPMSLVETILSEKKKLCLCAANKNELLCRGMNPNVPETLPKKIEVAVNEVLSSVNDTWATATTPTTFFTNPIILSAIAILVIVIIMVIIYLILRYRRKQKIKKKLQYIKLLKE
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (DNA 3'-5' helicase II) (G3XD04)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- UvrABC system protein A
- UvrABC system protein B
- UvrABC system protein C
- DNA mismatch repair protein MutL
- Formamidopyrimidine-DNA glycosylase
- Protein RecA
- Adenine DNA glycosylase
- DNA helicase RecQ
- DNA 3'-5' helicase II
- DNA polymerase I
Sequence:
MNDDLSLLLNSLNDPQRQAVAAPLGRQLVLAGAGSGKTRVLVHRIAWLIQVEHASPYSILSVTFTNKAAAEMRHRIEQLLGINPAGMWVGTFHGLAHRLLRAHWREAGLSENFQILDSDDQQRLVKRVIRELGLDEQRWPARQAQWFINGQKDEGLRPQHIQPGGDLFLATMLKIYEAYEAACARAGVIDFSELLLRALDLWRDHPGVLEHYQRRFRHILVDEFQDTNAVQYAWLRILAKGGDSLMVVGDDDQSIYGWRGARIENIQQFSDDFADAEVIRLEQNYRSTASILKAANALIANNQGRLGKELWTDGEDGESLSLYAAFNEHDEARYVVESIESALKGGLARSEIAILYRSNAQSRVLEEALLREKIPYRIYGGQRFFERAEIKNAMAYLRLLDGRGNDAALERVVNVPARGIGEKTVESIREFARGNDVSMWEAIRLMIANKVLPGRAASALTGFVELIENLSAKVMDMPLHLMTQTVIEQSGLISYHKEEKGEKGQARVENLEELVSAARAFENSEEEEDLTPLQAFLSHASLEAGETQADAHEDSVQLMTLHSAKGLEFPLVFLVGMEEGLFPHKMSLEESGRLEEERRLAYVGVTRAMQRLVLTYAETRRLYGSETYNKVSRFIREIPPALIQEVRLSNTVSRPYGGTSRSAGGNLFSGAGVPETPFSLGQRVRHALFGEGTILNFEGAGAQARVQVNFESEGSKWLMLGYAKLEAL
Protein: Serine protease inhibitor A3G (Serpin A3G) (Serine protease inhibitor 2A) (Serpin 2A) (Q5I2A0)
Organism: Mus musculus (Mouse)
Function: Serine and cysteine protease inhibitor. Can inhibit lysosomal papain-like proteases including the cathepsins B, G, H, K, L and V. Ineffective against elastase, granzyme A, granzyme B, or caspases 3, 8 or 9. Inhibition of cytoplasmic cathepsin B following release from the lysosome may protect cells from apoptosis. This may facilitate the survival of progenitor T-cells and the subsequent development of long term memory CD8 T-cells.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
Sequence:
MAGVSPAVFGCPDVTLGRNTAVREVQENVTSVDSLTLVSSNTDFAFSLYRKLVLKNPDENVVFSPFSICTALALLSLGAKSNTLKEILEGLKFNLTETPEPDIHQGFRYLLDLLSQPGNQVQISTGSALFIEKHLQILAEFKEKARALYQAEAFTADFQQPLKATKLINDYVSNHTQGKIKELISGLKESTLMVLVNYIYFKGKWKNPFDPNDTFKSEFYLDEKRSVIVSMMKTGYLTTPYFRDEELSCTVVELKYTGNASAMFILPDQGRMQQVEASLQPETLRKWKNSLKPRMIHELRLPKFSISTDYSLEHILPELGIREVFSTQADLSAITGTKDLRVSQVVHKAVLDVAETGTEAAAATGMAGVGCCAVFDFLEIFFNRPFLMIISDTKAHIALFMAKVTNPERSMNFPNGEGASSQRLESKRLCFGDPLCLIGQ
Protein: Ribulose-phosphate 3-epimerase (EC 5.1.3.1) (Ribulose-5-phosphate-epimerase) (Q8VEE0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Interaction partners:
- Ribose-5-phosphate isomerase
- Transketolase
- Transketolase-like protein 1
- Transketolase-like protein 2
- 6-phosphogluconate dehydrogenase, decarboxylating
- Xylulose kinase
- Transaldolase
- Eukaryotic translation initiation factor 3 subunit D
- GDH/6PGL endoplasmic bifunctional protein
- Triosephosphate isomerase
Sequence:
MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEAAQKRSLDR
Protein: Mitochondrial metalloendopeptidase OMA1 (EC 3.4.24.-) (Q5A663)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Protease that is part of the quality control system in the inner membrane of mitochondria (By similarity). Cleaves and thereby promotes the turnover of mistranslated or misfolded membrane protein (By similarity). Required for TOR signaling.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P36163}; Single-pass membrane protein {ECO:0000250|UniProtKB:P36163}.
Interaction partners:
- Glucose-induced degradation complex subunit
- Uncharacterized protein
- Proteasome maturation factor UMP1
- I-AAA protease
- Uncharacterized protein
Sequence:
MFGSKIFSRLFFKRTYATYKRFDNTTSSSSFTTSYAHLLTNRKTLYIGGGLLGFYVYNLHDAPYTHRSRFIWVPYWLETKIGDYSYRQIYQQFQSQILPHSNPLYNRVSTIMNKLLDVALNDNINDDLNARFLNHLKSLKWEINIIQNDSLPPNAFILPNGKIFIFSSIMPICKNEDGLATVLSHELSHQLAQHSSEQLSKQPIYMVLSTILYTITGVSWFNDLLINGVLTMSASREMESEADHIGCELLARACFNPQESINFWHRMSQAEKKAAGIVSQEGGYLNTWEFFSTHPATSRRIADIQKWMPQLLQIRESSGCYEYGRFYNFNKSYFSH
Protein: Retinoic acid receptor beta (RAR-beta) (Nuclear receptor subfamily 1 group B member 2) (P22448)
Organism: Gallus gallus (Chicken)
Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for limb and craniofacial development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Arginine--tRNA ligase, cytoplasmic
- Cytochrome P450 26A1
- Cytochrome P450 26B1
- Uncharacterized protein
- Mediator of RNA polymerase II transcription subunit 1
- Uncharacterized protein.
- Retinal dehydrogenase 2
- Aldehyde dehydrogenase 1A1
Sequence:
MTTSSRTCPVPAVNGHMTHYPAAPYPLLFPPVIGGLSLPSLHGLQSHPPTSGCSTPSPATVETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEPTKQESTENYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTSLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPMKVDKLQEPLLEALKIYIRKRRPNKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPTSNGNTAEHSPSISPSSVDNSSVSQSPMVQ
Protein: Chitooligosaccharidolytic beta-N-acetylglucosaminidase (EC 3.2.1.52) (Beta-GlcNAcase) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (P49010)
Organism: Bombyx mori (Silk moth)
Function: Active during metamorphosis to degrade chitin.
Interaction partners:
- Beta-galactosidase.
- Alpha-galactosidase.
- Alpha-galactosidase.
- Fucosyltransferase
- Hexosyltransferase.
- Uncharacterized protein.
- Sulfatase domain-containing protein.
- Uncharacterized protein
- Chitin-binding type-2 domain-containing protein
- Glyco_18 domain-containing protein
Sequence:
MWLQAICIYTVFIIIGCGIPTAAEEHSLWRWTCENNRCTKIRNEPENKEPVLSLEACKMFCDDYGLLWPKPTIETNLGNFLSKINMNTIDIQITKQGKSDDLLTAAADRFKTLVSSSVPKGFSAKAAGKSVTVYLVNENPYIREFSLDMDESYELYISSTSSDKVNATIRGNSFFGVRNGLETLSQLIVYDDIRNNLLIVRDVTIKDRPVYPYRGILLDTARNFYSIDSIKRTIDAMAAVKLNTFHWHITDSQSFPLVLQKRPNLSKLGAYSPTKVYTKQDIREVVEYGLERGVRVLPEFDAPAHVGEGWQDTGLTVCFKAEPWTKFCVEPPCGQLNPTKEELYDYLEDIYVEMAEAFESTDMFHMGGDEVSERCWNSSEEIQNFMIQNRWNLDKSSFLKLWNYFQKNAQDRAYKAFGKRLPLILWTSTLTDYTHVEKFLDKDEYIIQVWTTGADPQIQGLLQKGYRLIMSNYDALYFDCGFGAWVGSGNNWCSPYIGGQKVYGNSPAVMALSYRDQILGGEVALWSEQSDPATLDGRLWPRAAAFAERMWAEPSTAWQDAEHRMLHVRERLVRMGIQAESLEPEWCYQNQGLCYG
Protein: FI24025p1 (Frazzled, isoform A) (A1Z920)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Netrin-B
- Roundabout 1, isoform A
- Netrin receptor unc-5
- Protein slit
- Caspase-8
- Laminin subunit beta-1
- E3 ubiquitin-protein ligase TRIM9
- Moesin/ezrin/radixin homolog 1
- Tyrosine-protein kinase Abl
Sequence:
MAITTNRSSRTLWNWLLSSCLIFQLIGSSLASQALSFTLEPQDAVVPEGHSVLLQCAGTASIGRGGKSKSNLPSSVSIRWRGPDGQDLVIVGDTFRTQLKNGSLYISSVEENRGLTGAYQCLLTAEGVGSILSRPALVAIVRQPDLNQDFLETYLLPGQTAYFRCMLGEANWQEGVKHSVQWLKDDLPLPLDKLRMVVLPNGALEIDEVGPSDRGSYQCNVTSGSSSRLSSKTNLNIKKPSDPGAENSVAPSFLVGPSPKTVREGDTVTLDCVANGVPKPQIKWLRNGMDLDFNDLDSRFSIVGTGSLQISSAEDIDSGNYQCRASNTVDSLDAQATVQVQEPPKFIKAPKDTTAHEKDEPELKCDIWGKPKPVIRWLKNGDLITPNDYMQLVDGHNLKILGLLNSDAGMFQCVGTNAAGSVHAAARLRVVPQGVKIKKRKSQGHSTKSLQTFDNLTKRRKPFNSGEQLRTKSGGSFPFPDEDDDLDDNDSGTTRLRIPSGKLPKFEQPLNDRRFNILNAGSALPLDNQSKSYEDDDDDYDEDDPAKEALLEAYKQGEDAHKILDSWQQSKSKKSQQQKQSPASPDSPEQDPSVPHPGGKPLDSGLQARLPSQPRDLVAQIVKSRFVTLSWVEPLQNAGDVVYYTVYYKMNNSEREQKMVTKSHDDQQVNIQSLLPGRTYQFRVEANTNFGSGASSAPLEVSTQPEVNIAGPPRNFEGYARSHKEIYVKWEEPTVTNGEILKYRVYYSENDSGADLYHDSTALEAVLTELRPHTDYVISVVPFNRNGMGDSSAEIRVKTFSSTPSEPPNNVTLEVTSSSSITVHWEPPAEEDRNGQITGYKIRYRKFKDAPQVKSTPANIRYFELSNLDRNAEYQVKIAAMTVNGSGPFTEWNRANTLENDLDETQVPGKPIWISIHPGANNIALHWGPPQHPEIKIRNYVLGWGRGIPDENTIELKETERYHILKNLESNMDYVVSLRARNVKGDGPPIYDNIKTRDEEPVDAPTPLEVPVGLRAITMSSSSIVVYWIDTMLNKNQHVTDNRHYTVSYGITGSNRYRYHNTTDLNCMINDLRPNTQYEFAVKVVKGRRESSWSMSVLNSTYQNVPVTPPREVTVRLDEMNPPTVIVQWIPPKHTLGQITGYNIYYTTDTTKRDRDWSVEAFAGEETMLMLPNLKPYTTYYFKVQARTTKGANNAPFSALVSYTTSAAVTMQEPDTIAKGIDNEKLLYIIIAATAVVLLVVLLGVLLLCRRKPQSSPEHTKKSYQKNNVGVPKPPDLWIHHDQMELKNIDKGLHTVTPVCSDGASSSGALTLPRSVVHSEYEVETPVPGHVTNSLDKRSYVPGYMTTSMNGTMERPQYPRTQYSHQNRSHMTMEAGLSQQSLTQPQSNSMAQTPEHPYGGYDANFCNAGNAAAGNGCVSTIESSKRGHPLKSFSVPGPPPTGGATPVTKHTPAVTIRPQNQSPYKKPSFSAATPNRLQGGGSVVHSTDEIQRLAPSTSTEELNQEMANLEGLMKDLSAITANEFEC
Protein: Kinesin heavy chain 73, isoform D (EC 3.6.1.3) (A0A0B4KG24)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEKQQTILQNPPPLEKIERKQPKTFAFDHCFYSLNPEDENFASQETVFDCVGRGILDNAFQGYNACIFAYGQTGSGKSYTMMGTQESKGIIPRLCDQLFSAIANKSTPELMYKVEVSYMEIYNEKVHDLLDPKPNKQSLKVREHNVMGPYVDGLSQLAVTSYQDIDNLMTEGNKSRTVAATNMNAESSRSHAVFSVVLTQILTDQATGVSGEKVSRMSLVDLAGSERAVKTGAVGDRLKEGSNINKSLTTLGLVISKLADQSNGKKSGNDKFVPYRDSVLTWLLKDNLGGNSRTVMVATISPSADNYEETLSTLRYADRAKRIVNHAVVNEDPNARIIRELRHEVETLRSMLKHATGSPVGDVQDKLAESENLMKQISQTWEEKLVKTERIQNERQQALEKMGISVQASGIKVEKNKYYLVNLNADPSLNELLVYYLKDRTLIGGRTISGQQPDIQLSGLGIQPEHCVITIEDSGLYMEPVQGARCFVNGSAAVEKTPLQNGDRILWGNHHFFRVNSPKSNNTSMCASEPQTPAQLIDYNFARDEIMQNELSNDPIQTAIARLERQHEEDKQVALEKQRQEYERQFQQLRNILSPSTPYAPYAPYDPLRMGKITPNTPTSQMRVEKWAQERDEMFRRSLGQLKTDIMRANSLVQEANFLAEEMEKKTKFSVTLQIPPANLSPNRRRGAFVSEPAILVKRTNSGSQIWTMEKLENKLIDMREMYQEHKERVLNGLDEDNAKPQDPFYESQENHNLIGVANIFLEVLFHDVKLDYHTPIISQQGEVAGRLQVEIERIAGQMPQDRMCESVSESSGDSRDEYDDPVDPTSNQITCRVTIKCASGLPLSLSNFVFCQYTFWGHQEMVVPVINAESTAHDQNMVFKFEHTQDFTVTINEEFLEHCIEGALSIEVWGHRSAGFSKTKGWEVEQQQAKARSLVDRWAELSRKIELWVEIHELNDNGEYSPVEVTNRNEVLTGGIYQLRQGQQRRVNVRVKPVQNSGTLPIICQSIVNVAIGSVTVRSRLQRPLDSYQEEDLTVLREKWSEALGRRRQYLDQQIQMLIKKEEKNEQERERELSLVHQWVSLTEERNAVLVPAPGSGIPGAPASWEPPSGMEPHVPVLFLNLNGDDLSAQNTNDELSVAGINSILSKEHGHKFYTLQILQHLDKDVCCVASWDSSMHDSQALNRVTEANERVYLILRTTVRLSHPAPMDLVLRKRLSINIKKGQTLTDRLKKFRLVRGENAIWQSGVTYEVVSNIPKASEELEDRESLAQLAASGDDCSASDGETYIEKYTRGVSAVESILTLDRLRQNVAVKELETAHGQPLSMRKTVSVPNFSQAVKDTTNTGSQLINKLTQIMRFDASMESLLNVGRSESFADLNNSALGNKFTPGHSPAGAGGVIRSRHSFGGKGSSDDSPGKAFGIARPTFLNLNLNLNTLRIAPTKPSPATSKLLGMRMTTLHEEPLGGHRSLDEEPEDSYSDSEYAAEYEQERQQNKSMATRSRLTASKTMDSFMDVSSHSNQSYLSYTSSANANMKHLTGLATLSMSSSTSSGYGSQAVSCNNLSNEDIASMRSMSIDETPDFDRVNSNSPPNRQARVNPFLKDMPKAKIQEQPEQQAKKLQEAFTHPLEQLESSQNAQSDDDECAQLPKNNNNNLDLVNEPKPLSSQTDLEESMSQPKSKTEFATDNQNGNRSSDELSHSSEDLLEGDGIVREELPAGKVVRRKKSNTQPPSNGNSINNNNNGTTQAPRINHRASVAKMEGLAAYLDSSIMTSSTEVDEESKDVELVLPEWIVVGESVLIRPYNTSGVIRFVGTTEFQPGAWIGVELDTPTGKNDGSVKGVQYFQCKPKHGMFVRSDKLMLDKRGKAMRAYKAAEKSNSISKEMSTSMTGSMTRSKSRGDSLNLSARK
Protein: Malignant fibrous histiocytoma-amplified sequence 1 homolog (Q3V1N1)
Organism: Mus musculus (Mouse)
Function: Probable GTP-binding protein (By similarity). Functions in innate immunity and more specifically the inflammatory response as a regulator of the Toll-like receptor TLR2 and TLR4 signaling pathways. Negatively regulates the part of the TLR4 signaling pathway that leads to the activation of the transcription factor AP-1. By retaining the phosphatase complex PP2A into the cytoplasm, prevents the dephosphorylation of the AP-1 subunit JUN which is required for proper activation of the transcription factor (By similarity). Both inhibits and activates the TLR2-dependent signaling pathway. Positively regulates the TLR2 signaling pathway to activate specifically the downstream p38 and JNK MAP kinases and promote the polarization of macrophages toward the pro-inflammatory M1 phenotype. It may also play a role in the regulation of inflammation induced by high glucose through the PKB/AKT signaling pathway. Also involved in erythrocyte differentiation through activation of the ERK1/ERK2 signaling pathway (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4C4}.
Interaction partners:
Sequence:
MAGQDSGNLKTVRLWRDAALRARKLRSNLRQLTLSCPGAGGDPLESPDAPQLVLPANIGDIEVLNLGNNGLEDVPEGLGSALGSLRVLVLRRNRFARLPPAVAELGHHLTELDVSHNRLTILGAEVVSALRELRKLNLSHNQLPALPAQLGALAHLEELDVSFNRLAHLPDSFSCLNHLRTLDVDHNQLTAFPQQLLQLAALEELDVSSNRLRGLPEDISALRALKILWLSGAELGTLPRGFCELASLESLMLDNNGLQALPDEFSRLQRLKMLNLSSNLFEEFPAALLPLAGLEELYLSRNQLTSVPSLIAGLGRLLTLWLDNNRIRYLPDSIVELTGLEELVLQGNQIAVLPDNFGQLSRVGLWKIKDNPLIQPPYEVCMKGIPYIAAYQKELAHSQPAVQPRLKLLLMGHKAAGKTLLRHCLTEDKVEGGQGGGDKEKSYLPFPPLGSKGIEVTSWTADASRGLRFIVYDLAGDESYEVIQPFFLSPGALYVLVVNLATYEPRCFPTTVGSFLHRVGARVPHAVVCIVGTHADLCGERELEEKCLDIHRQIALQEKNDAEGLSHLAKVVDEALARDFELRSASPHAAYYGVSDKNLRRRKAHFQYLLNHRLQILSPVLPVSCRDPLQLQRLRDKLLSVAEHREIFPNLHRVLPRSWQVLEELHFQPPQAQRLWLSWWDSARLGLQAGLTEDRLQSALSYLHESGKLLYFEDSPALKEHVFHNLTRLIDILNVFFQRDASLLLHKLLLGTNGEGEGEGESFPTIAVPSPGQDPLRATQLHHYVEGFLLHGLLPAHIIRLLLKPHVQAQQDLQLLLELLEKMGLCYCLNKPKGKPLNGSAAWYKFPCYVQNEVPHAEAWINGTNLAGQSFVAEQLQIEYSFPFTFPPGLFARYSVQINSHVVHRSDGKFQIFAYRGKVPVVVSYRPAKGVLQPDTLSIASHASLPNIWTAWQAITPLVEELNVLLQEWPGLHYTVHILCSKCLKRGSPNPHAFPGELLSQPRPEGVAEIICPKNGSERVNVALVYPPTPTVISPCSKKNVGEKHRNQ
Protein: Inosine-5'-monophosphate dehydrogenase 1a (IMP dehydrogenase 1a) (IMPD 1a) (IMPDH 1a) (EC 1.1.1.205) (Q6GMG5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03156}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase isozyme 2
- 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase.
- Adenylosuccinate synthetase isozyme 1
- Adenylosuccinate synthetase
- AMP deaminase
- AMP deaminase
- AMP deaminase
- AMP deaminase
- Hypoxanthine phosphoribosyltransferase
Sequence:
MADYLISGGTGYVPEDGLTAQQLFAIGDGLTYNDFLILPGFIDFISDEVDLTSALTRKITLKTPLISSPMDTVTESSMAIAMALMGGIGIIHHNCTPEFQANEVRKVKKFEQGFITDPVVMSPRHTVGDVFEAKVRHGFSGIPVTETGKMGSKLVGIVTSRDIDFLSEKDYDRPLEESMTKREDLVVAPAGVTLKEANDILQRSKKGKLPIVNDSDELVAIIARTDLKKNRDYPLASKDSRKQLLCGAAIGTREDDKYRLDLLMQAGVDVIVLDSSQGNSVFQISMINYIKQKYPELQVVGGNVVTAAQAKNLIDAGVDALRVGMGCGSICITQEVMACGRPQGTSVYKVAEYARRFGVPVIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKNNSSQKRYFSEGDKVKVAQGVSGSVQDKGSIHKFVPYLIAGIQHGCQDIGAKSLSILRSMMYSGELKFEKRTMSAQVEGGVHGLHSYSFLPFTRNGYIEPGSRGHPRAGPNVPSPAVTKHSS
Protein: Phosphoglucomutase-1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1) (P36871)
Organism: Homo sapiens (Human)
Function: This enzyme participates in both the breakdown and synthesis of glucose.
Subcellular location: [Isoform 1]: Cytoplasm.
Interaction partners:
- Phosphopentomutase
- UTP--glucose-1-phosphate uridylyltransferase
- Glucose-6-phosphate isomerase
- Phosphoacetylglucosamine mutase
- 6-phosphogluconate dehydrogenase, decarboxylating
- 1,4-alpha-glucan-branching enzyme
- Alpha-enolase
- Glycogen phosphorylase, muscle form
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, brain form
Sequence:
MVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAVCPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVASATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWQKYGRNFFTRYDYEEVEAEGANKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISRNQGLRLIFTDGSRIVFRLSGTGSAGATIRLYIDSYEKDVAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT
Protein: Tachykinin-like peptide-XI (P.nigriventer tachykinin peptides XI) (PnTkP-XI) (U29-ctenitoxin-Pn1k) (U29-CNTX-Pn1k) (P86308)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKNDKKDRFYGLM
Protein: Myosin-ID light chain (Calmodulin-like protein mlcD) (Myosin light chain mlcD) (MlcD) (Q7Z2B8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Functions as the light chain for myosin-D. Has low affinity for calcium.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12826013}.
Interaction partners:
- Probable serine/threonine-protein kinase roco11
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase qkgA
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Inositol 1,4,5-trisphosphate receptor-like protein A
- Ras GTPase-activating-like protein gapA
Sequence:
MASKLNEEAQSEFKEGFALYDGNKDGKLEAAELANTLRWLGQNPSQSEINEILREFGSNNQMGVDGLFNYLGRKVVDDFDEKEIIEAFQVFDKDGKGMIGASDLRHILTNLGERLPEEQVEEMLRQAVGSGDGAINYEPFVRNMLKK