wanglab/gogpt-training-data huggingface dataset:
Protein: 3'3'-cGAMP-specific phosphodiesterase 3 (3'3'-cGAMP PDE 3) (V-cGAP3) (EC 3.1.4.-) (Q9KL18)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP), leading to linear 5'-pApG. Counteracts the function of the 3'3'-cGAMP synthase DncV, and is involved in the modulation of intracellular 3'3'-cGAMP levels. Enhances bacterial chemotaxis and inhibits intestinal colonization in vivo. Thus exerts a crucial role in regulating bacterial infectivity through catalyzing 3'3'-cGAMP degradation. Is specific for 3'3'-cGAMP since it cannot degrade other cGAMP linkage isomers (3'2'-, 2'3'-, and 2'2'-cGAMPs); is also able to hydrolyze c-di-GMP but not c-di-AMP.
Interaction partners:
- diguanylate cyclase
- Sensory box/GGDEF family protein
- diguanylate cyclase
- histidine kinase
- GGDEF family protein
- GGDEF family protein
- Aerobic respiration control sensor protein
- histidine kinase
- histidine kinase
- histidine kinase
Sequence:
MSVAQNTFPLSELMISLTTALDMTEGQPPEHCIRCCWIGMHIGMQLELSEPELHDLFFTLLLKDAGCSSNAARICELYATDDLTFKRRYKTVGTSLSSVINFIVKNTGSEQSWTERILTTIDILKNGNDYAQELIQTRCTRGADVARELRFSEAVAQGIHSLDEHWNGQGRPEQRKGEAIPLFSRIALLAQVFDVFQMEHSIEEALQEIMARSGVWFDPKLVEVVEQLVENPRFLSGLKATDISQRVMNLPPAQAHLPLDDAYLECIVTAFGKIVDAKSPYTAGHSERVAVYTDLIARQLAISDADRIWLRRAALLHDIGKLGVSNAILDKPGKLDEAEWRAVQAHAAYTEQILYKLSPFKTLARMAGAHHEKLDGTGYPRGVNGDEISLMTRIITTADIFDALSAERPYRAAMPIDKALAIMEENLHTAIDPECFAALKKALNLLPDEYTQLPHSSDKT
Protein: EARP-interacting protein homolog (Q86A97)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Vacuolar protein sorting-associated protein 51 homolog
- Vps53-like domain-containing protein
- Vacuolar protein sorting-associated protein 54
- Hisactophilin-2
Sequence:
MFNTNTSNISTNVYGLSQKTRALSHITAEADVNRFLVGTTALREENEIALLEAKEGEGVRCLSIFPHPKEIHSITSCPFDSSLFFSVYNTSGGGNNNSNNTNNNDNTNNNTNNNDFKSSLWRINESMDSIEELFELKGHTGIIKPILCDPSGSNNFIISLDDSNIRLWSKIDDQNEPTVIKQFGNLSKLSVGSINPNISNQLATANDVNIKGWDFRNAKETFSMDKAHSEQIRDIDFNPNKPYYLLSAGDDCKLKIWDTRQTRDPVKIFSGHNHWIWSAKFNRYHDQLIITSSSDNTVKLWNLYSLSSAFNSENNISNSNEQQHSQQPNEQQPQQPPQPVKQKKNKRNEDQLIKTYEEHEDSVYNISWSSSNFLFASLSYDGRFVVNNVPKEYSDILSYI
Protein: Plasma membrane low affinity zinc ion transporter, putative (Q4WHX5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362088}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362088}.
Interaction partners:
Sequence:
MQSLHTLLVRDPETGATPSCDTGNEYDGRMGLRISSIFVIMVGSMLGAVFPVFARSFSTSKFLRRAFFVAKYFGSGVIIATAFIHLLGPAEEALTNECLTGPITEYSWVEGIILMTIVVLFFVELMVMRYARFGHGHLDDLGHDDHTHPSLDAPPATVESKSHMPGEDHLGHSREHRDTESGRKASLIEEYSAQLTSVFILEFGIIFHSIFIGLTLAVSGEEFITLYIVLVFHQTFEGLGLGSRLATIPWPNSKRFTPYLLGFAYGLSTPLAIAIGLGVRNSYPPEGYTTLVVNGVFDSISAGILIYTALVELMAHEFMFSPSMRKAPIRTVLAAFGLLCLGALLMALLGKWA
Protein: GEO01111p1 (HL01263p) (RH26825p) (SKP1-related A, isoform A) (SKP1-related A, isoform B) (SKP1-related A, isoform C) (SKP1-related A, isoform E) (SKP1-related A, isoform F) (SKP1-related A, isoform G) (SKPA) (O77430)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- S-phase kinase-associated protein 2
- Cullin homolog 1
- Cullin 6
- Supernumerary limbs, isoform B
- RING-box protein 1A
- RING-box protein 1B
- Cullin 3, isoform F
- Ubiquitin-like protein NEDD8
- Calcyclin-binding protein
- Transcriptional activator cubitus interruptus
Sequence:
MPSIKLQSSDEEIFDTDIQIAKCSGTIKTMLEDCGMEDDENAIVPLPNVNSTILRKVLTWAHYHKDDPQPTEDDESKEKRTDDIISWDADFLKVDQGTLFELILAANYLDIKGLLELTCKTVANMIKGKTPEEIRKTFNIKKDFSPAEEEQVRKENEWCEEK
Protein: Calcium load-activated calcium channel (CLAC channel) (GEL complex subunit TMCO1) (Transmembrane and coiled-coil domain-containing protein 1) (Q921L3)
Organism: Mus musculus (Mouse)
Function: Calcium-selective channel required to prevent calcium stores from overfilling, thereby playing a key role in calcium homeostasis. In response to endoplasmic reticulum (ER) overloading, assembles into a homotetramer, forming a functional calcium-selective channel, regulating the calcium content in endoplasmic reticulum store. Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (By similarity). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions (By similarity). Within the MPT complex, the GEL subcomplex may mediate insertion of transmembrane regions into the membrane (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UM00}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UM00}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UM00}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UM00}. Mitochondrion membrane {ECO:0000250|UniProtKB:C5HGF3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UM00}. Note=The first transmembrane region is required for localization to the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9UM00}.
Interaction partners:
- PAT complex subunit CCDC47
- Phenylalanine--tRNA ligase beta subunit
- BOS complex subunit TMEM147
- BOS complex subunit NCLN
- ER membrane protein complex subunit 3
- GEL complex subunit OPTI
- Protein transport protein Sec61 subunit gamma
- Protein transport protein Sec61 subunit alpha isoform 2
- Growth arrest-specific protein 7
Sequence:
MSTMFADTLLIVFISVCTALLAEGITWVLVYRTDKYKRLKAEVEKQSKKLEKKKETITESAGRQQKKKIERQEEKLKNNNRDLSMVRMKSMFAIGFCFTALMGMFNSIFDGRVVAKLPFTPLSYIQGLSHRNLLGDDTTDCSFIFLYILCTMSIRQNIQKILGLAPSRAATKQAGGFLGPPPPSGKFS
Protein: SH3 domain containing ring finger 2 (Q08AM8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDDLTLLDLLECPVCFEKLDVTAKVLPCQHTFCKPCLQRVFKAHKELRCPECRTPVFSNIEALPANLLLVRLLDGVRSGQSSGRGGSFRRPGTMTLQDGRKSRTNPRRLQASPFRLVPNVRIHMDGVPRAKALCNYRGQNPGDLRFNKGDIILLRRQLDENWYQGEINGISGNFPASSVEVIKQLPQPPPLCRALYNFDLRGKDKSENQDCLTFLKDDIITVISRVDENWAEGKLGDKVGIFPILFVEPNLTARHLLEKNKGRQSSRTKNLSLVSSSSRGNTSTLRRGPGSRRKVPGQFSITTALNTLNRMVHSPSGRHMVEISTPVLISSSNPSVITQPMEKADVPSSCVGQVSTYHPAPVSPGHSTAVVSLPGSQQHLSANMFVALHSYSAHGPDELDLQKGEGVRVLGKCQDGWLRGVSLVTGRVGIFPNNYVIPIFRKTSSFPDSRSPGLYTTWTLSTSSVSSQGSISEGDPRQSRPFKSVFVPTAIVNPVRSTAGPGTLGQGSLRKGRSSMRKNGSLQRPLQSGIPTLVVGSLRRSPTMVLRPQQFQFYQPQGIPSSPSAVVVEMGSKPALTGEPAFTCISRGSEARIHSAASSLIMEDKEIPIKSEPLPKPPASAPPSILVKPENSRNGIEKQVKTVRFQNYSPPPTKHYTSHPTSGKPEQPATLKASQPEAASLGPEMTVLFAHRSGCHSGQQTDLRRKSALGKATTLVSTASGTQTVFPSK
Protein: Signal recognition particle receptor subunit beta (Q9VSN9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Signal recognition particle receptor subunit alpha homolog
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP72
- Signal recognition particle 54 kDa protein
- Signal recognition particle 14 kDa protein
- Signal recognition particle 19 kDa protein
- DSec61alpha
- Serine/threonine-protein kinase ATR
- Signal recognition particle 9 kDa protein
- Large ribosomal subunit protein eL31
Sequence:
MDKLNENARQRKQIKLGEIDTGPIIVALLLGFIAVAIFVILRRRSAGRKDFLLTGLSESGKSAIFMQLIHGKFPATFTSIKENVGDYRTGSASARLVDIPGHYRVRDKCLELYKHRAKGIVFVVDSVTAHKDIRDVADFLYTILSDSATQPCSVLVLCNKQDQTTAKSAQVIKSLLESELHTVRDTRSRKLQSVGDEDGSKSITLGKPGRDFEFSHIAQNIQFAEASAKDTELDPLTDWLARLL
Protein: Zinc finger protein 423 homolog (O/E-associated zinc finger protein) (Protein Lobe) (A1Z9R4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable transcription factor that can both act as an activator or a repressor depending on the context (By similarity). Involved in posterior spiracle development. Acts downstream of ems and cut in posterior spiracle development.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MMALKMLYRGPSSRLENLIEKIQATKEITNNDMYSTHTSSSYSPSISDGTMTPNSHHLIGAPTAAGQEDHPTEGKINGGADGEDLPKPKRLPHFHHHHHHHYHHQQALKIANKLRKINKEAKMGATAGGGATGAASKFDKLTGEGIKSRGDGSYQCQFCEKTFPRLGYLKHHVQSHAEHLPFKCEYCSKLFKHKRSRDRHKKLHTNERNYKCPHCEAAFSRSDHLKIHMKTHDIQKPFQCSMCNRGYNTAAALTSHMQKHKKNAAILAAGGNPNALNYSPRSTGSASASVSSNGSLQKRRYALALASDSSPSRMDFPKRSRSNHVGGTTTTATPTPLLRCSYCPKVTEFSSLEQLNAHLQSVHEQPQTQAVKTPVQEGEGFQLSCEYCTMKFGNIAGLFQHMRSTHMDRLSSPNSYYEHFNRLATAGTFSPRLALDLPKIKPDLGSPERESRPAEDDLPTDLSNNKRRPLTPNPQAQTPLAPPSAPPGVFFCNQCNAGLPDFESFRNHLKSHIAEGMQLVCPHCGMSLPEQSEFERHVVGHFLITGSEFNCSSSCGKSFAKSEDLQQHLLSEHVLTLLKCSLCSELCESRMAMQLHLACAHSQETKLLRCSACLELFRSDAEFHVHVKTRHQLGGHPTLGATSSAPTNPLQCMFCRAVCSSELEMHFHLAAHARQFRCPSCPETFHVEFLLDRHMQSQHGGVKDKEANSPNMGSLYVNALLPPLAAAAAAAAATNNNSSIIDYNVAFKGLFGGASGGAGSGGGGAQSGGAPPSANKFYSPLQVDTNALKAQTSPHPALMYGLSQRYLMEMYAAKSTSPSGNEGVGNSQPPAPQATAPPPPPNASTATFSCGMCERQDLRSEAELHSHRKLAHNLKTGVSLRCAYCAGNFKSRAELEQHMKSCHNSTGKHKCLICDEVFPSPAILAEHKLQHSKVGQSGKCSHCGQPLEDVAAFRAHLSEHGSDGASLPLACICCRQTLHSEFELSLHAKFHTKSSSSGGSLQEPVCALCLEPLPDATEGPAKLCDKCCRKHNLNGKRGKHSEPATSLPAPPSAFVENRCNLCKMILPHAQKLQEHLVEHTFAGTEQRGFNCYICSAVFTAPGGLLNHMGEHGAHSRPYDCNLCPEKFFFRAELEHHQRGHELRPQARPPAAKVEVPSIRNTSPGQSPVRSPTIVKQELYETDTVESAGVEDEPENHPDEEEYIEVEQMPHETRPSGIGSQLERSTSSA
Protein: Suppressor of kinetochore protein 1 (P19/Skp1 homolog) (Q9Y709)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cig2 degradation in the G2 and M phases of the cell cycle. Together with pof6, essential for septum processing and cell separation. Involved in mitotic progression, essential for the execution of anaphase B; required for coordinated structural alterations of mitotic spindles and segregation of nuclear membrane structures at anaphase. Involved in the DNA damage checkpoint pathway and maintenance of genome integrity. Component of the RAVE complex which is required for stable assembly of the vacuolar ATPase complex V-ATPase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12167173, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:12167173, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cullin-1
- RING-box protein pip1
- F-box DNA helicase protein 1
- F-box/WD repeat-containing protein pof1
- SCF E3 ubiquitin ligase complex F-box protein pof2
- WD repeat-containing protein pop2
- WD repeat-containing protein pop1
- F-box protein pof7
- F-box/TPR repeat protein pof3
- F-box/WD repeat-containing protein pof11
Sequence:
MSKIKLISSDNEEFVVDQLIAERSMLIKNMLEDVGEINVPIPLPNVSSNVLRKVLEWCEHHKNDLYSGTEEESDIRLKKSTDIDEWDRKFMAVDQEMLFEIVLASNYLDIKPLLDTGCKTVANMIRGKSPEDIRKTFNIPNDFTPEEEEQIRKENEWAEDR
Protein: Myocardin (Basic SAP coiled-coil transcription activator 2) (SRF cofactor protein) (Q8VIM5)
Organism: Mus musculus (Mouse)
Function: Smooth muscle cells (SM) and cardiac muscle cells-specific transcriptional factor which uses the canonical single or multiple CArG boxes DNA sequence. Acts as a cofactor of serum response factor (SRF) with the potential to modulate SRF-target genes. Plays a crucial role in cardiogenesis, urinary bladder development, and differentiation of the smooth muscle cell lineage (myogenesis). Isoform 1 mediates the cardiac transcription factor MEF2C-dependent transcription. Isoform 1 and isoform 3 are more active than isoform 2 and isoform 4 in stimulating cardiac muscle promoters.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:15601857}. Note=Nuclear, with a punctate intranuclear pattern with exclusion from nuclei.
Interaction partners:
- Serum response factor
- T-box transcription factor TBX5
- Histone deacetylase 5
- Transcription factor GATA-4
- Myocyte-specific enhancer factor 2C
- Myosin-11
- Homeobox protein Nkx-2.5
- Transgelin
- Krueppel-like factor 4
- Calponin-1
Sequence:
MTLLGSEHSLLIRRKFRSVLQLRLQQRRTQEQLANQGLIPPLKGPTEFHDPRKQLDSAKTEDSLRRKGRNRSDRASLVTMHILQASTAERSIPTAQMKLKRARLADDLNEKIALRPGPLELVEKNILPMDSSVKEAIKGTEVSLSKAADAFAFEDDSSRDGLSPDQARSEDPQGSTGSTPDIKSTEAPLDTIQDLTPGSESDKNDAASQPGNQSDPGKQVLGPLSTPIPVHTAVKSKSLGDSKNRHKKPKDPKPKVKKLKYHQYIPPDQKAEKSPPPMDSAYARLLQQQQLFLQLQILSQQQQQQQQQQQQQQQQQQQQQRFSYPGMHQTHLKEPNEQMARNPNPSSTPLSNTPLSPVKNSISGQTGVSSLKPGPLPPNLDDLKVSELRQQLRIRGLPVSGTKTALVDRLRPFQDCAGNPVPNFGDITTVTFPVTPNTLPSYQSSPTGFYHFGSTSSSPPISPASSDLSAAGSLPDTFTDASPGFGLHASPVPACTDESLLSSLNGGSGPSEPDGLDSEKDKMLVEKQKVINQLTWKLRQEQRQVEELRMQLQKQKSSCSDQKPLPFLATTIKQEDVSSCPFAPQQASGKGQGHSSDSPPPACETAQLLPHCVESSGQTHVLSSTFLSPQCSPQHSPLGGLKSPQHISLPPSPNNHYFLASSSGAQRENHGVSSPSSSQGCAQMTGLQSSDKVGPTFSIPSPTFSKSSSAVSDITQPPSYEDAVKQQMTRSQQMDELLDVLIESGEMPADAREDHSCLQKIPKIPGSSCSPTAIPPKPSASFEQASSGGQMAFDHYANDSDEHLEVLLNSHSPIGKVSDVTLLKIGSEEPPFDSIMDGFPGKAAEDLFSAHELLPGPLSPMHAQLSPPSVDSSGLQLSFTESPWETMEWLDLTPPSSTPGFSNLTSSGPSIFNIDFLDVTDLNLNSPMDLHLQQW
Protein: Phosphatidylcholine synthase (PC synthase) (PCS) (EC 2.7.8.24) (CDP-diglyceride-choline O-phosphatidyltransferase) (A9CIM3)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP. Affects motility, biofilm formation and virulence of this bacterium when there is a complete loss of phosphatidylcholine formation due to absence of both the synthase (pcs) and the methylation (pmtA) pathways.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:Q9KJY8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9KJY8}.
Interaction partners:
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidate cytidylyltransferase
- Methyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
Sequence:
MKIFNYKRVPYAEIRAFSVHILTASGSFLAFLGVVAASEHRFVDMFWWLGLALLVDGIDGPIARKVRVKEVLPNWSGDTLDNIIDYVTYVLLPAFALYQSGMIGEPLSFVAAGMIVVSSAIYYADMGMKTDEYFFSGFPVVWNMVVFTLFVMDASATTAMTVVTVSVFLTFLPINFLHPVRVKRLRPLNLLVVAIWCALGGYALLMHFETPTWAVIAFVASGIYLYCIGGILQFFPSLGAK
Protein: Phosphate-specific transport system accessory protein PhoU homolog 1 (Pst system accessory protein PhoU homolog 1) (P9WI97)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Plays a role in the regulation of phosphate uptake. In this role, it may bind, possibly as a chaperone, to PhoR, PhoP or a PhoR-PhoP complex to promote dephosphorylation of phospho-PhoP, or inhibit formation of the PhoR-PhoP transitory complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphate import ATP-binding protein PstB 2
- Phosphate transport system permease protein PstA 1
- Phosphate import ATP-binding protein PstB 1
- RNA pseudouridylate synthase
- Phosphate transport system permease protein PstA 2
- Possible esterase lipoprotein LpqC
- Phosphate transport system permease protein PstC 1
- Glycerol-3-phosphate dehydrogenase 2
- Phosphate transport system permease protein PstC 2
- Probable conserved Mce associated membrane protein
Sequence:
MRTVYHQRLTELAGRLGEMCSLAGIAMKRATQALLEADIGAAEQVIRDHERIVAMRAQVEKEAFALLALQHPVAGELREIFSAVQIIADTERMGALAVHIAKITRREYPNQVLPEEVRNCFADMAKVAIALGDSARQVLVNRDPQEAAQLHDRDDAMDDLHRHLLSVLIDREWRHGVRVGVETALLGRFFERFADHAVEVGRRVIFMVTGVLPTEDEISTY
Protein: DMXL1 protein (B2RWN7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNLHQVLTGAVNPGDHCFSVGSIGDQRFTAYASGCDIVILGSDFERLQIIPGAKHGNIQVGCVDCSMQQGKIAASYGNVISIFEPVNLPKQKKNLELYSQWQKSGQFFLESIAHNITWDPTGSRLLTGSSYLQLWSNTNLEKPTEDENLNKTDLNFGDWKCIWHCKTASQVHLMKFSPDGEFFATAGKDDCLLKVWYNVENWRTAVTSPDGSSEKQSQGEIDFSFVYLAHPRAVNGFSWRKTSKYMPRASVCNVLLTCCKDNVCRLWVETFLPNDCLLYGGDCSHWTESINLTNNFKRNASSKERVQNALEVNLRHFRRGRRRSLALVAHTGYLPHQQDPHHVHRNTPLHANALCHFHIAASINPATDIPLLPSITSLSLNENEEKTGPFVVHWLNNKELHFTLSMEVFLQQLRKSFEQPSSEASVEDSNQADVKSDEETDDGVDDLKINPEKKELGCDKMVPNSSFTSLSSAAIDHQIEVLLSEWSKNADMLFSIHPMDGSLLVWHVDWLDEYQPGMFRQVQVSFVSRIPVAFPTGDANSLCKSIMMYACTKNVDLAIQQGKQKPSGLTRSTSMLISSGHNKSSNSLKLSIFTPNVMMISKHADGSLNQWLVSFAEESAFSTVLSISHKSRYCGHRFHLNDLACHSVLPLLLTTSHHNALRTPDVDNPEQPFDALNIEECSLTQQNKSTVDVAFQDPSAVYSELILWRVDPVGPLSFSGGVSELARINSLHVSAFSNVAWLPTLIPSYCLGAYCNSPSACFVASDGQYLRLYEAVIDAKKLLSELSNPEISKYVGEVFNIVSQQSTARPGCIIALDPITKLHGRKTQLLHVFEEDFILNNLEKKSLGKDSILSNAGSSPNGFSEKFYLIVIECTQDNRSLLHMWNLHLKSIPVSLDEKVDTKLSEAVWQPEEHYSSSPEKILSPFSQKYQACRANLQSTSRLTLFSEMVYSQELHLPEGVEIISIKPSAGHLSSSSIYPACSAPYLLATSCSDEKVRFWRCRVTDGESATSKNGKIDLAYIWEEWPLLIEDGLQSNSSITVPGRPVEVSCAHTNRLAVAYKQPASNSRSSQDFVMHVSIFECESTGGSCWVLEQTIHLDELSTVLDSGISVDSNLVAYNKQDMYLSSKENITSNTKHLVHLDWMSREDGSHILTVGIGSKLFMYGPLAGKVQDQTGKETLAFPLWESTKVVPLSKFVLLRSVDLVSSVDGSPPFPVSLSWVRDGILVVGMDCEMHVYCQWQPSSKQEPVITDSYSGSTPSITSLIKQSNSSSGLHPPKKTLTRSMTSLAQKICGKKTAFDPSVDMEDSGLFEAAHVLSPTLPQYHPLQLLELMDLGKVRRAKAILSHLVKCIAGEVVALNEAESNHERRLRSLTISASGSTTRDPQAFNKAENTDYTEIDSVPPLPLYALLAADDDSCYSSLEKSSNESTLSKSNQLSKESYDELFQTQLLMTDTHMLETDEENTKPRVIDLSQYSPTYFGPEHAQVLSGHLLHSSLPGLSRMEQMSLMALADTIATTSTDIGESRDRSQGGETLDECGLKFLLAVRLHTFLTTSLPAYRAQLLHQGLSTSHFVWAFHSVAEEELLNMLPAMQKDDPTWSELRAMGVGWWVRNTRILRKCIEKVAKAAFYRKNDPLDAAIFYLAMKKKAVIWGLYRAEKNTRMTQFFGHNFEDERWRKAALKNAFSLLGKQRFEHSAAFFLLAGCLRDAIEVCLEKLNDIQLALVIARLYESEFDTSAAYKSILRKKVLGIDSPVSELCSLNINMHHDPFLRSMAYWILEDYSGALETLIKQPIRENDDQVLSASNPTVFNFYNYLRTHPLLLRRHFGSSDTFSTHMSLTGKSGLAGTINLSERRLFFTTASAHLKAGCPMLALEVLSKMPKVIKKTRPFYRASSFLDTSKDCSPSSPLKLDAREDKSSAVDWSQSLINGFGSSSEGSSEKQSNSTLSFDWSQPSVVFQDDSLELKWDSDNDEENEDVPISMKELKPLQRKTDKKLDDISSNYTESFSTLDENDLLNPSEDIIAVQLKFRACLKILTVELRTLSTGYEIDGGKLRYQLYHWLEKEVIALQRTCDFCSDAEELQSAFGRNEDEFGLNEDAEDLPHQTKVKQLRENFQEKRQWLLKYQSLLRMFLSYCILHGSHGGGLASVRMELILLLQESQQETSEPLFSSPLSEQTSVPLLFACTANAKTVVANPLLHLSNLTHDILHAIINFDSPPHPDIQSNKVYVMHTLAASLSACIYQCLCGSHNYSSFQTNQFTGMVYQTVLLPHRPSLKTGSLDEALTPNTSPAQWPGITCLIRLLNSSGEEAQSGLTVLLCEILTAVYLSLFIHGLATHSSNELFRIVAHPLNEKMWSAVFGGGAHVPSKEQTHSKTLPVSSLVEEGEKQNKRFRPSKMSCRESAPLTPSSAPVSQESLAVKEKFIPPELSIWDYFIAKPFLPSSQSRAEYDSEESLGSDDDDNDDDDDVLASDFHLQEHSNSNSYSWSLMRLAMVQLVLNNLKTFYPFAGHDLAELPVSSPLCHAVLKTLQCWEQVLLRRLEIHGGPPQNYIASHTAEESLSAGPAILRHKALLEPTNTPFKSKHHLALSVKRLWQYLVKQEEIQETFIKNIFTKKRCLNESLEDNSETIKNSMMEEPNINKIEADLGYPGGKARIIHKESDIITAFAVNKANRNCIAIASSHDVQELDVSGILATQVYTWVDDDIEVETKGSEDFLVIHARDDLTAVQGTTPYTHSNPGTPINMPWLGSTQTGRGASVMIKKAINNVRRMTSHPTLPYYLTGAQDGSVRMFEWGHSQQITCFRSGGNSRVTRMRFNYQGNKFGIVDADGYLSLYQTNWKCCPVTGSMPKPYLTWQCHNKTANDFVFVSSSSLIATAGLSTDNRNVCLWDTLVAPANSLVHAFTCHDSGATVLAYAPKHQLLISGGRKGFTYVFDLCQRQQRQLFQSHDSPVKAVAVDPTEEYFVTGSAEGNIKIWSLSTFGLLHTFVSEHARQSIFRNIGTGVMQIETGPANHIFSCGADGTMKMRILPDQFSPLNEVLKNDVKFML
Protein: Apolipoprotein D (Apo-D) (ApoD) (P51910)
Organism: Mus musculus (Mouse)
Function: APOD occurs in the macromolecular complex with lecithin-transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein A-II
- Apolipoprotein A-I
- Clusterin
- Apolipoprotein A-IV
- Apolipoprotein E
- Apolipoprotein C-I
- Apolipoprotein F
- Apolipoprotein M
- Apolipoprotein B-100
- Apolipoprotein C-II
Sequence:
MVTMLMFLATLAGLFTTAKGQNFHLGKCPSPPVQENFDVKKYLGRWYEIEKIPASFEKGNCIQANYSLMENGNIEVLNKELSPDGTMNQVKGEAKQSNVSEPAKLEVQFFPLMPPAPYWILATDYENYALVYSCTTFFWLFHVDFVWILGRNPYLPPETITYLKDILTSNGIDIEKMTTTDQANCPDFL
Protein: Possible transcriptional regulatory protein (P96812)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible transcriptional regulatory protein
- Putative cytochrome P450 138
Sequence:
MTAVAAGALVVETDSFRLRLLDGLVASIGERGYRATTVSDIVRHARTSKRTFYDRFTSKEQCFLELLLADNETLGNSIRAAVDPNADWHDQIRQAVEAYVTHIESRPAVTLSWIREFPSLGAAAYPVQRRGMEQLTSLLIELSASPGFRRANLPPLNVPLAVILLGGLRELTALTVEDGQPIRNIVEPAVDASIALLGPRS
Protein: Suppressor of cytokine signaling at 16D, isoform A (Q9VX18)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDSSIKLKDSNSNCSSNSNGNVGGGGVAGGGGSGSGGVCVSSICSSDSFSIMPPPHHELVSANSIELNAAASLSDDSGVPLTTNSSISSGDSYRLGMCKFEIEMVESDGEVSQFDSLDNCSEGGMSAENFNTLKKGPLAPIDPPPEFQDSPQTTLVRSISKNIVNSLRRWTSSQSSFEHLKDDATTMVSGLATAVLPEEPHPPSQELVLLLAKTECKLDALDGQALGQMSLKESYAINKHLYSSDSILNSHTDNIYDEPNNIVSSSLGNSVDLLDEEQSDASSCSPLPSPPPPVSIVKIKQTLCPYYQDHTRYFKAIPTEQDNIASAKAAAAQQRFNSAGLSEIHDYDLYYGARRQPVDNSSLQRRQASLYSPLGHTSHCHYHHSHGHGHGSHHHHHHHQPGYGYSHGQRPNSRNSLNSRLSSSHNSLNVSSANKPDDSIFITQAMSHDALFTREISDFYNVPIDSDIYAFPVDMIEQQQQQQLLVEEQQQQKPAAPTYHKASRRNKRNKRKQRYAGSGTGAGTETSDGDGEKSKHGKYRTPVGVGMGQVSESEPLHMTLDEVKQFYHTLYSDAGKPTPKPMVKSSNETIWSVSTNTTTTTARTRSSVGTTRGGGGPPGAGNGAGGASSDGGVGGGSAGGGGGKYLSKQNKHNLDNDKLNNNNNNNNNHQPSQQQLEKPPTEHHNQHQPPNNKHVLHSEKKSQFTLNLKQRFCSIFRFRRSNHSRCRGSGNNQTGTFASANANAAATAPLIPPIAVITSAPGAAGQTQLASELNGTLITAEADEPNADLRKKFQSRALPPLPKKAAAYAIEAVKSEPEEVKTNAIQEPRALQFTSSIEKVKDYGWYWGPLSSEAAEKVLSSEPDGSFIVRDSSDDHYIFSLSFKLNNCVRHVRIEQDQGTFSFGSYAKFKSQTITEFIEKAVEHSRSGRYLFFLHRRPEHGPMRVQLTNPVSRFKHVQSLQHMCRFVILKAVIRKDLIQTLPLPRRLLDYLNYKHCYSEQVESDSSHSQISGDGTM
Protein: 18S rRNA (guanine-N(7))-methyltransferase bud23 (EC 2.1.1.-) (Bud site selection protein 23 homolog) (Q10162)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Multifunctional methyltransferase subunit trm112
- Uncharacterized protein C13G1.09
- Ribosome biogenesis protein tsr1
- 25S rRNA
- 20S-pre-rRNA D-site endonuclease nob1
- Protein LTV1
- Small ribosomal subunit protein uS5
- Pre-rRNA-processing protein pno1
- tRNA
- eRF1 methyltransferase catalytic subunit mtq2
Sequence:
MSRPEHIAPPEIFYNDVEAGKYSTNTRIQSIQTEMSERALELLDAEGPSFILDIGCGSGISTQIGESQGHVVVGMDISPSMLSVALESQEIEGDLLLCDMGTGVPFRPGTFDGVISISAIQWLLNADKTCNVPQRRLNRFFQTLYISMKRGGRAVMQYYPETEKSQQMIMDTARKAGFAGGIVVDHPESKRQKKYYLVLQAGGTRTLDISSMTLDQEGTNAKQRKLKKKQDMSTREYIIHKKELNRKRGRLHVPKDSKYSGRRRKAAF
Protein: Lactosylceramide alpha-2,3-sialyltransferase (EC 2.4.3.9) (CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase) (GM3 synthase) (Ganglioside GM3 synthase) (ST3Gal V) (ST3GalV) (Sialyltransferase 9) (Q9UNP4)
Organism: Homo sapiens (Human)
Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of glycosphingolipids forming gangliosides (important molecules involved in the regulation of multiple cellular processes, including cell proliferation and differentiation, apoptosis, embryogenesis, development, and oncogenesis). Mainly involved in the biosynthesis of ganglioside GM3 but can also use different glycolipids as substrate acceptors such as D-galactosylceramide (GalCer), asialo-GM2 (GA2) and asialo-GM1 (GA1), although less preferentially than beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer (LacCer).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- Beta-1,4-galactosyltransferase 6
- Beta-hexosaminidase subunit beta
- Beta-hexosaminidase subunit alpha
- Beta-galactosidase
- Alpha-2,8-sialyltransferase 8E
Sequence:
MRTKAAGCAERRPLQPRTEAAAAPAGRAMPSEYTYVKLRSDCSRPSLQWYTRAQSKMRRPSLLLKDILKCTLLVFGVWILYILKLNYTTEECDMKKMHYVDPDHVKRAQKYAQQVLQKECRPKFAKTSMALLFEHRYSVDLLPFVQKAPKDSEAESKYDPPFGFRKFSSKVQTLLELLPEHDLPEHLKAKTCRRCVVIGSGGILHGLELGHTLNQFDVVIRLNSAPVEGYSEHVGNKTTIRMTYPEGAPLSDLEYYSNDLFVAVLFKSVDFNWLQAMVKKETLPFWVRLFFWKQVAEKIPLQPKHFRILNPVIIKETAFDILQYSEPQSRFWGRDKNVPTIGVIAVVLATHLCDEVSLAGFGYDLNQPRTPLHYFDSQCMAAMNFQTMHNVTTETKFLLKLVKEGVVKDLSGGIDREF