wanglab/gogpt-training-data huggingface dataset:
Protein: Transcriptional regulatory protein SIN3 (P22579)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the RPD3 histone deacetylase complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SIN3 has also a RPD3 independent function required for normal longevity.
Subcellular location: Nucleus.
Interaction partners:
- Transcriptional regulatory protein SDS3
- Transcriptional regulatory protein RCO1
- Transcriptional regulatory protein UME6
- Histone deacetylase RPD3
- Transcriptional regulatory protein UME1
- Transcriptional regulatory protein SAP30
- Chromatin modification-related protein EAF3
- Transcriptional regulatory protein PHO23
- Transcriptional regulatory protein RXT3
- Histone deacetylase complex subunit CTI6
Sequence:
MSQVWHNSNSQSNDVATSNDATGSNERNEKEPSLQGNKPGFVQQQQRITLPSLSALSTKEEDRRDSNGQQALTSHAAHILGYPPPHSNAMPSIATDSALKQPHEYHPRPKSSSSSPSINASLMNAGPAPLPTVGAASFSLSRFDNPLPIKAPVHTEEPKSYNGLQEEEKATQRPQDCKEVPAGVQPADAPDPSSNHADANDDNNNNENSHDEDADYRPLNVKDALSYLEQVKFQFSSRPDIYNLFLDIMKDFKSQAIDTPGVIERVSTLFRGYPILIQGFNTFLPQGYRIECSSNPDDPIRVTTPMGTTTVNNNISPSGRGTTDAQELGSFPESDGNGVQQPSNVPMVPSSVYQSEQNQDQQQSLPLLATSSGLPSIQQPEMPAHRQIPQSQSLVPQEDAKKNVDVEFSQAISYVNKIKTRFADQPDIYKHFLEILQTYQREQKPINEVYAQVTHLFQNAPDLLEDFKKFLPDSSASANQQVQHAQQHAQQQHEAQMHAQAQAQAQAQAQVEQQKQQQQFLYPASGYYGHPSNRGIPQQNLPPIGSFSPPTNGSTVHEAYQDQQHMQPPHFMPLPSIVQHGPNMVHQGIANENPPLSDLRTSLTEQYAPSSIQHQQQHPQSISPIANTQYGDIPVRPEIDLDPSIVPVVPEPTEPIENNISLNEEVTFFEKAKRYIGNKHLYTEFLKILNLYSQDILDLDDLVEKVDFYLGSNKELFTWFKNFVGYQEKTKCIENIVHEKHRLDLDLCEAFGPSYKRLPKSDTFMPCSGRDDMCWEVLNDEWVGHPVWASEDSGFIAHRKNQYEETLFKIEEERHEYDFYIESNLRTIQCLETIVNKIENMTENEKANFKLPPGLGHTSMTIYKKVIRKVYDKERGFEIIDALHEHPAVTAPVVLKRLKQKDEEWRRAQREWNKVWRELEQKVFFKSLDHLGLTFKQADKKLLTTKQLISEISSIKVDQTNKKIHWLTPKPKSQLDFDFPDKNIFYDILCLADTFITHTTAYSNPDKERLKDLLKYFISLFFSISFEKIEESLYSHKQNVSESSGSDDGSSIASRKRPYQQEMSLLDILHRSRYQKLKRSNDEDGKVPQLSEPPEEEPNTIEEEELIDEEAKNPWLTGNLVEEANSQGIIQNRSIFNLFANTNIYIFFRHWTTIYERLLEIKQMNERVTKEINTRSTVTFAKDLDLLSSQLSEMGLDFVGEDAYKQVLRLSRRLINGDLEHQWFEESLRQAYNNKAFKLYTIDKVTQSLVKHAHTLMTDAKTAEIMALFVKDRNASTTSAKDQIIYRLQVRSHMSNTENMFRIEFDKRTLHVSIQYIALDDLTLKEPKADEDKWKYYVTSYALPHPTEGIPHEKLKIPFLERLIEFGQDIDGTEVDEEFSPEGISVSTLKIKIQPITYQLHIENGSYDVFTRKATNKYPTIANDNTQKGMVSQKKELISKFLDCAVGLRNNLDEAQKLSMQKKWENLKDSIAKTSAGNQGIESETEKGKITKQEQSDNLDSSTASVLPASITTVPQDDNIETTGNTESSDKGAKIQ
Protein: UDP-D-xylose:beta-D-glucoside alpha-1,3-D-xylosyltransferase (EC 2.4.2.42) (Q9VBY3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Xyloside xylosyltransferase 1
- Uncharacterized protein, isoform J
Sequence:
MQHLHMCLLCLIALAILSYFVHQRPSWVTENKGKMLGYNELQTGKPPLYIVVVSCGQRVQETLVMIKSAILFNYDEEYLKFVIFTEDGKGDEFREKLTDWRDIKPFTFDFEILPLKFPSGNEVEWRNLFKPCAAQRLFLPSLLTHVDSLLYVDTDILFLSPISDIWRFFKKFNETQMSALTPEHENENIGWYNRFARHPFYGRLGVNSGVMLMNLTRMREMKWEQHIVSIHKEYKLRIIWGDQDIINILFYYHPDKLYIMPCEYNYRPDHCMYMSICNMSQTGVKVIHGNRGYFHSDRQPLFKSIYGAMENYQLGSNANTEFLMPLHAALSIPSIKNSSCGKISNEVLKVANAVVTKRYREV
Protein: Glutathione transporter 1 (O14031)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: High-affinity glutathione transporter which plays a role in scavenging glutathione from the extracellular environment for the maintenance of sulfur homeostasis.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Probable peptide transporter ptr2
- E3 ubiquitin-protein ligase ubr11
Sequence:
MTARNSASIPTSIRKTSENEVSGDETPAGVGNLSTKTASKTSLTFRQSSSDESTSSYSGNHHNINIQHHPNRPFRTNSSSFSPNDYSISESPSKSKKDGVHVSAVQLDNETDSEVESEVEELERELEAIEDSVYPEVRAAVNPTDDVNLPVNTWRTWVLTTIFVIVFAAVNQFFSLRYPALSISFIVAQLILFPLGKLLNLLPNWKIGYGRFSFYLNSSPFNVKEHAAITIAVSLTSSTAYATNILSAQTSFYKQNLSWGYKILIVLTSQMLGYGFAGLTRRWIVYPAAMIWPQTLVSTVLFRTLHGNSGNDIGVLKNNRISANGWTISRYRFFAYVMIGSFVFYWFPGFIFKGLSYFTVLCWIWPKNRVVNQLFGYNSGLGILPLTFDWQQVVYNSNPLASPWWVICNTFGSVVLIFWIVVPILYYKGVWFSNYLPMLSSSTFDHTGVSYNSSRVLNSDYSFNHTKYESYSPLYMPMSYSMSTALNFAAVTAIFTHCALYNGKDIWQRLWKESGKDECIHRKLMRNYKEAPQWWYATLFIVVFGLTIFTVRYYDTQCPVWALIVALLIFIVNFIPQGVLEGITNQHVGLNIITELIGGYILPGKPLANLMIKLYGFIPMRQGLEFSRDLKLAQYMKIPPRILFFVQLFATILGGITQVAVQEWMNYHIPGICTTSQSNGFTCPNGRSIYNASLIWGAIGPAKMFSKGKPYYPLIFFFLIGAVAPFITWGLRKRFPKSWIGKLNAPVLFTGPGNIPPATGINYSSWAIVGFIFNYVIRKRAIHWWRKYNYVLAAAMDSGVAVAGVVIFLCVSYPGGKITWWGNTVYTKTYDWKSVPYRSLGPNETFGYTNW
Protein: Mannosyltransferase regulator 4 (P36044)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May function as a positive regulator for mannosylphosphate transferase. Is required to mediate mannosylphosphate transfer in both the core and outer chain portions of N-linked oligosaccharides.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:30842360}; Single-pass type II membrane protein {ECO:0000255}. Note=Endoplasmic reticulum exit to the Golgi apparatus requires SVP26 and MNN6. {ECO:0000269|PubMed:30842360}.
Interaction partners:
- Mannosyltransferase KTR6
- Alpha-1,3-mannosyltransferase MNN1
- Alpha-1,2-mannosyltransferase MNN2
- Initiation-specific alpha-1,6-mannosyltransferase
- Alpha-1,2-mannosyltransferase MNN5
- Glycolipid 2-alpha-mannosyltransferase
Sequence:
MLQRISSKLHRRFLSGLLRVKHYPLRRILLPLILLQIIIITFIWSNSPQRNGLGRDADYLLPNYNELDSDDDSWYSILTSSFKNDRKIQFAKTLYENLKFGTNPKWVNEYTLQNDLLSVKMGPRKGSKLESVDELKFYDFDPRLTWSVVLNHLQNNDADQPEKLPFSWYDWTTFHELNKLISIDKTVLPCNFLFQSAFDKESLEAIETELGEPLFLYERPKYAQKLWYKAARNQDRIKDSKELKKHCSKLFTPDGHGSPKGLRFNTQFQIKELYDKVRPEVYQLQARNYILTTQSHPLSISIIESDNSTYQVPLQTEKSKNLVQSGLLQEYINDNINSTNKRKKNKQDVEFNHNRLFQEFVNNDQVNSLYKLEIEETDKFTFDKDLVYLSPSDFKFDASKKIEELEEQKKLYPDKFSAHNENYLNSLKNSVKTSPALQRKFFYEAGAVKQYKGMGFHRDKRFFNVDTLINDKQEYQARLNSMIRTFQKFTKANGIISWLSHGTLYGYLYNGMAFPWDNDFDLQMPIKHLQLLSQYFNQSLILEDPRQGNGRYFLDVSDSLTVRINGNGKNNIDARFIDVDTGLYIDITGLASTSAPSRDYLNSYIEERLQEEHLDINNIPESNGETATLPDKVDDGLVNMATLNITELRDYITSDENKNHKRVPTDTDLKDLLKKELEELPKSKTIENKLNPKQRYFLNEKLKLYNCRNNHFNSFEELSPLINTVFHGVPALIPHRHTYCLHNEYHVPDRYAFDAYKNTAYLPEFRFWFDYDGLKKCSNINSWYPNIPSINSWNPNLLKEISSTKFESKLFDSNKVSEYSFKNLSMDDVRLIYKNIPKAGFIEVFTNLYNSFNVTAYRQKELEIQYCQNLTFIEKKKLLHQLRINVAPKLSSPAKDPFLFGYEKAMWKDLSKSMNQTTLDQVTKIVHEEYVGKIIDLSESLKYRNFSLFNITFDETGTTLDDNTEDYTPANTVEVNPVDFKSNLNFSSNSFLDLNSYGLDLFAPTLSDVNRKGIQMFDKDPIIVYEDYAYAKLLEERKRREKKKKEEEEKKKKEEEEKKKKEEEEKKKKEEEEKKKKEEEEKKKKEEEEKKKQEEEEKKKKEEEEKKKQEEGEKMKNEDEENKKNEDEEKKKNEEEEKKKQEEKNKKNEDEEKKKQEEEEKKKNEEEEKKKQEEGHSN
Protein: Alpha-mammal toxin AnCra1 (C0HLG5)
Organism: Androctonus crassicauda (Arabian fat-tailed scorpion)
Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against mammals (Ref.1). The recombinant toxin selectively inhibits the fast inactivation of hNav1.7/SCN9A channel (EC(50)=136.7 nM). Is potent in inhibiting the fast inactivation of hNav1.7 and has little effect on the steady-state inactivation. In vivo, intravenous injection into mice induces muscle contraction, leading to severe paralysis and death (Ref.1).
Subcellular location: Secreted {ECO:0000269|Ref.1}.
Interaction partners:
Sequence:
LKDGYIVDDVNCTYFCGRNAYCNEECIKLKGESGYCQWASPYGNACYCYKLPDHVRTKGPGRCN
Protein: Large ribosomal subunit protein eL24 (60S ribosomal protein L24) (60S ribosomal protein L30) (P83731)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Small ribosomal subunit protein eS6
- Ubiquitin-ribosomal protein eL40 fusion protein
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL23
Sequence:
MKVELCSFSGYKIYPGHGRRYARTDGKVFQFLNAKCESAFLSKRNPRQINWTVLYRRKHKKGQSEEIQKKRTRRAVKFQRAITGASLADIMAKRNQKPEVRKAQREQAIRAAKEAKKAKQASKKTAMAAAKAPTKAAPKQKIVKPVKVSAPRVGGKR
Protein: Stromelysin-1 (SL-1) (EC 3.4.24.17) (EMS-2) (Matrix metalloproteinase-3) (MMP-3) (Transin-1) (P28862)
Organism: Mus musculus (Mouse)
Function: Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9. Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway. Acts also intracellularly. For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage. In addition, plays a role in immune response and possesses antiviral activity against various viruses. Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Osteopontin
- Metalloproteinase inhibitor 1
- Metalloproteinase inhibitor 2
- Interstitial collagenase B
- Matrix metalloproteinase-9
- Stromelysin-2
- Matrilysin
- Metalloproteinase inhibitor 3
- Nucleolar transcription factor 1
- Interleukin-6
Sequence:
MKGLPVLLWLCVVVCSSYPLHDSARDDDAGMELLQKYLENYYGLAKDVKQFIKKKDSSLIVKKIQEMQKFLGLEMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYAPGPGINGDAHFDDDERWTEDVTGTNLFLVAAHELGHSLGLYHSAKAEALMYPVYKSSTDLSRFHLSQDDVDGIQSLYGTPTASPDVLVVPTKSNSLEPETSPMCSSTLFFDAVSTLRGEVLFFKDRHFWRKSLRTPEPEFYLISSFWPSLPSNMDAAYEVTNRDTVFIFKGNQFWAIRGHEELAGYPKSIHTLGLPATVKKIDAAISNKEKRKTYFFVEDKYWRFDEKKQSMEPGFPRKIAEDFPGVDSRVDAVFEAFGFLYFFSGSSQLEFDPNAKKVTHILKSNSWFNC
Protein: Protein phosphatase Slingshot (EC 3.1.3.16) (EC 3.1.3.48) (Q6NN85)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor tsr/cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Required for axon growth.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Cofilin/actin-depolymerizing factor homolog
- LIM domain kinase 1
Sequence:
MALVTVQRSPSVAGSCSNSDGESEDDEGNSKGNDRSECFFAGKGTALVLALKDIPPLTQSERRLSTDSTRSSNSTQSNNSDIQLHLQSMFYLLQREDTLKMAVKLESQRSNRTRYLVIASRSCCRSGTSDRRRHRIMRHHSVKVGGSAGTKSSTSPAVPTQRQLSVEQTATEASSKCDKTADKENATAAGDNKNTSGMEESCLLGIDCNERTTIGLVVPILADTTIHLDGDGGFSVKVYEKTHIFKPVSVQAMWSALQTLHKVSKKARENNFYASGPSHDWLSSYERRIESDQSCLNEWNAMDALESRRPPSPDAIRNKPPEKEETESVIKMKLKAIMMSVDLDEVTSKYIRGRLEEILDMDLGEYKSFIDAEMLVILGQMDAPTKIFEHVYLGSEWNASNLEELQKNGVRHILNVTREIDNFFPGTFEYFNVRVYDDEKTNLLKYWDDTFRYITRAKAEGSKVLVHCKMGVSRSASVVIAYAMKAYQWEFQQALEHVKKRRSCIKPNKNFLNQLETYSGMLDAMKNKEKLQRSKSETNLKSTKDARLLPGSEPTPLIQALNQAKSKSTGEAGVTPDGEEEDGSRMHRRSIAQKSQRRMVRRSSSTSPKTQTAVVTKQQSQSMENLTPERSVAEEPKNMRFPGSNGENYSVTQNQVLHIQKHTPLSVRTRIHDLEAHRADQLPQQPVWTSLTKLITQTSHLGKSVSGSSSGNIDSRRDSSCSDVFSSQVDSVFAKDEGEKRQRRKTHSWTESLGPSGGIVLDPTPQQQKQQSNAILRPRGTRQRELPSRHASWGSGDNRCCLPQRTSSGSYYDSNRNTTAIFEGVIQDLKRSSNCNVIEGVAVAVEPIVGVGEGTVKRTKQKLEESTSLKKRCQEESQELLLEAVDAGQRRCPSLYRSASSAHSPRQRQPLRCNSEELMHTSDIENKNTTPGDHEATVVLRVQGQTLADDQRISGNVQILKQNFEAKAGVVGTGGGGGGGTAAGSGSSSTIATSVSAVAGACSANPGKKTTSHQSLPSSPVAQHANHVSAASNSNSSASNSSDSS
Protein: Protein phosphatase 1D (EC 3.1.3.16) (Protein phosphatase 2C isoform delta) (PP2C-delta) (Protein phosphatase magnesium-dependent 1 delta) (p53-induced protein phosphatase 1) (O15297)
Organism: Homo sapiens (Human)
Function: Involved in the negative regulation of p53 expression. Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins. Mediates MAPK14 dephosphorylation and inactivation. Is also an important regulator of global heterochromatin silencing and critical in maintaining genome integrity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:28343630, ECO:0000269|PubMed:9177166}. Cytoplasm, cytosol {ECO:0000269|PubMed:28343630}.
Interaction partners:
- Serine-protein kinase ATM
- Serine/threonine-protein kinase Chk2
- Amyloid protein-binding protein 2
- Cellular tumor antigen p53
- E3 ubiquitin-protein ligase Mdm2
- Runt-related transcription factor 2
- Histone H2AX
- Serine/threonine-protein kinase Chk1
- Core-binding factor subunit beta
- Protein Mdm4
Sequence:
MAGLYSLGVSVFSDQGGRKYMEDVTQIVVEPEPTAEEKPSPRRSLSQPLPPRPSPAALPGGEVSGKGPAVAAREARDPLPDAGASPAPSRCCRRRSSVAFFAVCDGHGGREAAQFAREHLWGFIKKQKGFTSSEPAKVCAAIRKGFLACHLAMWKKLAEWPKTMTGLPSTSGTTASVVIIRGMKMYVAHVGDSGVVLGIQDDPKDDFVRAVEVTQDHKPELPKERERIEGLGGSVMNKSGVNRVVWKRPRLTHNGPVRRSTVIDQIPFLAVARALGDLWSYDFFSGEFVVSPEPDTSVHTLDPQKHKYIILGSDGLWNMIPPQDAISMCQDQEEKKYLMGEHGQSCAKMLVNRALGRWRQRMLRADNTSAIVICISPEVDNQGNFTNEDELYLNLTDSPSYNSQETCVMTPSPCSTPPVKSLEEDPWPRVNSKDHIPALVRSNAFSENFLEVSAEIARENVQGVVIPSKDPEPLEENCAKALTLRIHDSLNNSLPIGLVPTNSTNTVMDQKNLKMSTPGQMKAQEIERTPPTNFKRTLEESNSGPLMKKHRRNGLSRSSGAQPASLPTTSQRKNSVKLTMRRRLRGQKKIGNPLLHQHRKTVCVC
Protein: cytochrome-c oxidase (EC 7.1.1.9) (Q9I3G3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Cytochrome c oxidase, cbb3-type, CcoO subunit
- Cbb3-type cytochrome c oxidase subunit
- Cytochrome c oxidase, cbb3-type, CcoO subunit
- Cbb3-type cytochrome c oxidase subunit
- Cytochrome c oxidase, cbb3-type, CcoQ subunit
- Probable ferredoxin
- Probable iron-sulfur protein
- Probable oxidoreductase
- Cytochrome b
- Urease accessory protein UreH-like transmembrane domain-containing protein
Sequence:
MSTAISQTAYNYKVVRQFAVMTVVWGVIGMGLGVLIAAQLVWPELNFDLPWTSFGRLRPLHTNAVIFAFGGCALFATSYYVVQRTSQARLISDTLAAFTFWGWQAVIVGAVLTLPQGFTTSKEYAELEWPLAILLAIVWITYAIVFFGTIVKRKVKHIYVGNWFYGAFILVTAMLHIVNHMSLPVSWFKSYSAYSGATDAMVQWWYGHNAVGFFLTTGFLGMMYYFVPKQAERPVYSYRLSIVHFWALISLYIWAGPHHLHYTALPDWAQSLGMVMSLILLAPSWGGMINGMMTLSGAWHKLRTDPILRFLVVSLAFYGMSTFEGPMMAIKTVNALSHYTDWTIGHVHAGALGWVAMISIGSLYHLIPKVFGRPQMHSIGLINAHFWLATIGTVLYIASMWVNGITQGLMWRAVNEDGTLTYSFVEALVASHPGFIVRMIGGGFFLTGMLLMAYNTWRTVRAAKPAEYEAAAQIA
Protein: Nuclear receptor subfamily 1 group H member 3 (C9J4R0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLWLGAPVPDIPPDSAVELWKPGAQDASSQAQGGSSCILREEARMPHSAGGTAGVGLEAAEPTALLTRAEPPSEPTEIRPQKRKKGPAPKMLGNELCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKGAHYICHSGGHCPMDTYMRRKCQECRLRKCRQAGMREECVLSEEQIRLKKLKRQEEEQAHATSLP
Protein: Collectin-11 (Collectin kidney protein 1) (CL-K1) (Q3SXB8)
Organism: Mus musculus (Mouse)
Function: Lectin that plays a role in innate immunity, apoptosis and embryogenesis. Calcium-dependent lectin that binds self and non-self glycoproteins presenting high mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope. Primarily recognizes the terminal disaccharide of the glycan. Also recognizes a subset of fucosylated glycans and lipopolysaccharides. Plays a role in innate immunity through its ability to bind non-self sugars presented by microorganisms and to activate the complement through the recruitment of MAPS1. Also plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding. Finally, plays a role in development, probably serving as a guidance cue during the migration of neural crest cells and other cell types during embryogenesis.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9BWP8}.
Interaction partners:
- Collectin-10
- Mannan-binding lectin serine protease 1
- Mannan-binding lectin serine protease 2
- Complement C1r-A subcomponent
- Complement C1s-1 subcomponent
- C-type lectin domain family 12 member A
- Ficolin-1
- Mannose-binding protein C
- Ficolin-2
- Complement C1s-1 subcomponent
Sequence:
MMMRDLALAGMLISLAFLSLLPSGCPQQTTEDACSVQILVPGLKGDAGEKGDKGAPGRPGRVGPTGEKGDMGDKGQKGTVGRHGKIGPIGAKGEKGDSGDIGPPGPSGEPGIPCECSQLRKAIGEMDNQVTQLTTELKFIKNAVAGLRETESKIYLLVKEEKRYADAQLSCQARGGTLSMPKDEAANGLMASYLAQAGLARVFIGINDLEKEGAFVYSDRSPMQTFNKWRSGEPNNAYDEEDCVEMVASGGWNDVACHITMYFMCEFDKENL
Protein: Altered inheritance of mitochondria protein 3 (P38266)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane raft {ECO:0000269|PubMed:15561700}; Peripheral membrane protein {ECO:0000269|PubMed:15561700}. Note=Localize within detergent-insoluble glycolipid-enriched membranes.
Interaction partners:
- Reduced viability upon starvation protein 161
- Reduced viability upon starvation protein 167
- Actin cytoskeleton-regulatory complex protein SLA1
- Myosin tail region-interacting protein MTI1
- Actin-binding protein
- Protein YSC84
- Proline-rich protein LAS17
- Altered inheritance of mitochondria protein 4
- Protein AIM2
- LAS seventeen-binding protein 5
Sequence:
MGFWENNKDSITSGLKSAGKYGYQGTKYVAKTGYKASKKHYNNSKARRERKSGKKNSSDEEYDSEDEMEYERKPTDIRSLKDPKSFPPPPLKPGQKTYTGQQQQQMPNGQASYAFQGAYQGQPGAGSTEQSQYAQPQYNQYPQQQLQQGVMPQQQQLQQGVVPQQPPIYGEQVPPYGSNSNATSYQSLPQQNQPQNAIPSQVSLNSASQQSTGFVSQNLQYGTQSSNPAPSPSFQNGLQCHQQPQYVSHGSTNLGQSQFPSGQQQQPTTQFGQQVLPSPAQPQQQQQGQPLPPPRGQVILPAPGEPLSNGFGQQQQQQQQQQQPLNQNNALLPQMNVEGVSGMAAVQPVYGQAMSSTTNMQDSNPSYGASPMQGQPPVGGQPPVPVRMQPQPPQPMQQGNIYPIEPSLDSTGSTPHFEVTPFDPDAPAPKPKIDIPTVDVSSLPPPPTHRDRGAVVHQEPAPSGKIQPNTTSSAASLPAKHSRTTTADNERNSGNKENDESTSKSSILGHYDVDVNIMPPPKPFRHGLDSVPSEHTTKNAPERAVPILPPRNNVEPPPPPSRGNFERTESVLSTNAANVQEDPISNFLPPPKPFRHTETKQNQNSKASPVEMKGEVLPGHPSEEDRNVEPSLVPQSKPQSQSQFRRAHMETQPIQNFQPPPKPFRRSQSSNSSDSSYTIDGPEANHGRGRGRIAKHHDGDEYNPKSENSTENGRLGDAPNSFIRKRAPTPPAPSRSEKLHEGTITSEVDSSKDANKYEKSIPPVTSSIQAQQSTKKAPPPVVKPKPRNFSLKANEYPKELTREATGQDEVLNSITNELSHIKLRKTNVNLEKLGGSKKVKDSSPVPSDLDEKYVSASGSITPPRPPPSRSSPKKVPPVVPKKNDNLKKKPPVVPKKKPLLKSLEPRPIEMERAYSGDISAADDNLNPFERYKRNVVPQEDDRLHKLK
Protein: cGMP-dependent protein kinase, isozyme 2 forms cD5/T2 (cGK) (EC 2.7.11.12) (Foraging protein) (P32023)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKIKHYPGKAVDASLSLEGSSAMGALYEANWLRAANQPAAPATTGTKLSRQSSSAGSSFLIEGISALSKYQMTLENIRQLELQSRDKRIASTIKELSGYRPSALQHHQQQQMHNVWVAEDQDQEHEELEDASEGKEKLASIQEPPAVNHYVLDPTERPRVPRPRQQFSVKPPSLRRSQTMSQPPSYATLRSPPKIKENLSKSSSAYSTFSSAAEDSQDQVVICQQPQRLMAPPPREPPPEPPKRVSKPLSRSQTSVQRYATVRMPNQTTSFSRSVVRSRDSTASQRRLSLEQAIEGLKLEGEKAVRQKSPQISPAASSNGSSKDLNGEGFCIPRPRLIVPVHTYARRRRTGNLKEQSSGGQEEEAEKGKGWKDFYVLSQDRHSSFYINRIGQNYDYDYPINFNIFSPDGRVEVSREGKYLSTLSGAKVLGELAILYNCQRTATITAITECNLWAIERQCFQTIMMRTGLIRQAEYSDFLKSVPIFKDLAEDTLIKISDVLEETHYQRGDYIVRQGARGDTFFIISKGKVRVTIKQQDTQEEKFIRMLGKGDFFGEKALQGDDLRTANIICESADGVSCLVIDRETFNQLISNLDEIKHRYDDEGAMERRKINEEFRDINLTDLRVIATLGVGGFGRVELVQTNGDSSRSFALKQMKKSQIVETRQQQHIMSEKEIMGEANCQFIVKLFKTFKDKKYLYMLMESCLGGELWTILRDKGNFDDSTTRFYTACVVEAFDYLHSRNIIYRDLKPENLLLNERGYVKLVDFGFAKKLQTGRKTWTFCGTPEYVAPEVILNRGHDISADYWSLGVLMFELLTGTPPFTGSDPMRTYNIILKGIDAIEFPRNITRNASNLIKKLCRDNPAERLGYQRGGISEIQKHKWFDGFYWWGLQNCTLEPPIKPAVKSVVDTTNFDDYPPDPEGPPPDDVTGWDKDF
Protein: Rifin (Q8IFK8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFELPLNILIYNQRNHYITRTPKTNTRTLCECELYAPSNYDNDQEMKEVMQQFEVRTSQRFHEYDESLQSKRMQCKDKCDKEIQKIILKDKLEKELMDKFATLQTDIQNDAIPTCVCEKSLADKVEKTCLKCGGLLGGGVAPGWGLISGLGYVGWTNYVTQTALQKGIEAVISYLEQIPGITDLPGFNLANIINPKNYSSSSLIIQAIDAAAGPICDVPVNESLKFCVLSSYNESTIIKQVSGGAESAAAFGEETASAEVAKFVPKTTILTNTITTSFIVIVVIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: V-1 protease (Q9Q2G4)
Organism: Human immunodeficiency virus type 1 (HIV-1)
Interaction partners:
Sequence:
PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMNLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF
Protein: Sulfotransferase 1B1 (ST1B1) (cSULT1B1) (EC 2.8.2.1) (Sulfotransferase family cytosolic 1B member 1) (Q95JD5)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43704}.
Interaction partners:
Sequence:
MISPKDFLRKNLKMIHGYPIIYTFANNWENIEQFHSRPDDIIIATYPKSGTTWVSEIVDMVLNNGDVEKCKRDFITVKVPMLEMAVPGLRTSGIEQLEKNPSPRLVKTHLPIALLPKSFWENNCKMIYLARNAKDVAVSYYHFDLMNNLEPAPGPWEEYLERFMTGNVAYGSWFNHVKSWWKKKEEHPILFLYYEDMKENPKREVQKIARFLEKNLNDEVLDKIIHHTSFEMMKDNPLVNYTHLPSTVMDHSKSSFMRKGIAGDWKNYFTVAQNEKFDVIYKKEMSGTTLQFRTEI
Protein: Protein lin-7 homolog (Q8IMT8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cell membrane {ECO:0000256|ARBA:ARBA00004202, ECO:0000256|PIRNR:PIRNR038039}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202, ECO:0000256|PIRNR:PIRNR038039}.
Interaction partners:
- Protein PALS1
- Protein crumbs
- Patj homolog
- LD29223p
- Moesin/ezrin/radixin homolog 1
- Atypical protein kinase C
- Peripheral plasma membrane protein CASK
- Cadherin-86C
- Zyx102 protein
- Protein limb expression 1 homolog
Sequence:
MADNAEPLTLSRDVKRSIELLEKLQASGDFPTTKLAALQKVLNSDFMTSVREVYEHVYETVDIQGSHDVRASATAKATVAAFAASEGHAHPRVVELPKTEEGKTRPYELRIEGIPLYHKTNTLIVKVYRPRIYVSIIHLIWKALSIFNFCFSGLGFNVMGGKEQNSPIYISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGENHEKAVELLKQAVGSVKLVVRYTPKVLEEMEMRFDKQRNTRRRQ
Protein: Mitochondrial 2-oxodicarboxylate carrier 1 (Q03028)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transports C5-C7 oxodicarboxylates across the inner membranes of mitochondria. Can transport 2-oxoadipate, 2-oxoglutarate, adipate, glutarate, 2-oxopimelate, oxaloacetate, citrate and malate. The main physiological role is probably to supply 2-oxoadipate and 2-oxoglutarate from the mitochondrial matrix to the cytosol where they are used in the biosynthesis of lysine and glutamate, respectively, and in lysine catabolism.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- Mitochondrial 2-oxodicarboxylate carrier 2
- Citrate/oxoglutarate carrier protein
Sequence:
MTSIDNRPLPFIYQFTAGAIAGVSELLVMYPLDVVKTRMQLQVTTKGHPAVVAAKAAVDHYTGVMDCLTKIVKKEGFSHLYKGITSPILMEAPKRAIKFSGNDTFQTFYKKIFPTPNGEMTQKIAIYSGASAGAVEAFVVAPFELVKIRLQDVNSQFKTPIEVVKNSVVKGGVLSLFNGLEATIWRHVLWNAGYFGIIFQIRKLLPAAKTSTEKTRNDLIAGAIGGTVGCLLNTPFDVVKSRIQRSSGPLRKYNWSLPSVLLVYREEGFKALYKGFAPKVMRLAPGGGLLLVVFTNVMDFFREVKYGKKQ