wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (O61651)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADEKAKESFRERQAQELEVIKSIFGCDVEDLRPQANPSLWKPTDIRIQLTPLRDSSNGLETYVCTKLHVTCPSKYPKLPPKISLEESKGMSDQLLEALRNQLQAQSQELRGEVMIYELAQTVQAFLLEHNKPPKGSFYDQMLQDKQKRDQELQDIQRQRESLQRQTLIDEVERRKEMFKTEAKRRGEPRRSMSESNPRHPSSSESSENSSPYYRGHIYPSKCLDHRNTETLYFHKMGRQIQRGCCVGHSQRGCIAYTGIDMHCGQLLYITEWNIKYSQLEQPCIGGGKCHWSSESKCMGSHRVDEVMASIEKQVSSLSQLQHKNLVSYECVLCIKRKEGLLVYLVQDFLLGTSVFSISSSLGWCMDGARMVARGVLDALVFLHNKGVSHSHLLDTTVFMDNTGNVRVSDFSLVPNLLELLSGAGQSSSCGDLPALGALVESLMPTNSYEMRDFVDKCNSDRTLSASELLEHPFLRFYVDNGQQQVMPLPQQQHPNTVQRTGSAMPYQIPTLALSQSRLRTEFEVLMYLGKGAFGDVLKVRNILDNREYAIKRIPLPARSRQLYKKMTREVELLSRLNHENVVRYFNSWIESVDDADAAEMDKLLGGEWSQSQQDLSVKPAKSPQLGPTLEEDEDEEDSSSSMWNGYIPNMEDSDSDGIEFVDSNGKVAVYDDEEQEDSTRGKTNSPKPLMQVMYIQMEFCEKCTLRTAIDDNLFNDTDRLWRLFREIAEGLAHIHQQGIIHRDLKPVNIFLDSHDQIKIGDFGLATTSFLALQAHDAAPAPVNQITSAEDGTGTGKVGTTLYVAPELTGNASKSVYNQKVDMYTLGIILFEMCQPPFDTSMERAQTIMALRNVSINIPDAMLKDPKYEKTVKMLQWLLNHDPAQRPTAEELLISDLVPPAQLEANELQEMLRHALANPQSKAYKNLVARCLQQESDEVLEHTYHLGSSRAMKSWNSAIIIDDIVSLNPVIEFVKAKVVNLFRKHGAIEVDSPLLSPLSARNSTANANANAVHLMTHSGCVVVLPCDLRTQFARHVTMNSVNLIRRYCVDRVYREERVFNFHPKQSYDCSFDIIAPTTGSHLVDAELLSLAFEITSELPRLREKNLAIRMNHTNLLRAILIFCNVPKAQYGALFEGTMDFIESRISRFQFHSSITGIMEKSRTSAQTLMDMLLANFLLTGSRSTVDDSALKSLMRGKGEAASLARGALRELETVVGLAYSLGVKCPIHIWAGLPISFDRASNGGIVWQMTADLKPNRSGHPSVLAIGERYDSMLHEFQKQAQKFNPAMPARGVLSGAGLTFSLDKLVAAVGVEYAKDCRAIDVGICVCGTRPPLKDVTYIMRLLWSVGIRCGIVEAASELGDEAQDLARLGALHVILVAENGSLRVRSFERERFQERHLTRTELVEFIQKMLRSDGLNGTTVDNFSHLSALGSGDNRSSGGKERERGENGLSTSASNATIKNNYSQLPNLQVTFLTHDKPTANYKRRLENQVAQQMSSTLSQFLKKETFVVLVVELPPAVVNAIVGAINPREIRKRETEPEINYVIERFSKYKRYISEINEEVVDYLSDAKTPIVALYSISDSYYRVII
Protein: Coatomer subunit alpha (Alpha-coat protein) (Alpha-COP) (HEP-COP) (HEPCOP) [Cleaved into: Xenin (Xenopsin-related peptide); Proxenin] (P53621)
Organism: Homo sapiens (Human)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.; SUBCELLULAR LOCATION: [Xenin]: Secreted {ECO:0000250}.
Interaction partners:
- Coatomer subunit epsilon
- Coatomer subunit beta'
- Coatomer subunit delta
- Coatomer subunit beta
- Coatomer subunit zeta-1
- Coatomer subunit gamma-1
- Coatomer subunit gamma-2
- Coatomer subunit zeta-2
- N-terminal kinase-like protein
- Transmembrane emp24 domain-containing protein 10
Sequence:
MLTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPTEDLVVSASLDQTVRVWDISGLRKKNLSPGAVESDVRGITGVDLFGTTDAVVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKAWEVDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLNLFAAGHDGGMIVFKLERERPAYAVHGNMLHYVKDRFLRQLDFNSSKDVAVMQLRSGSKFPVFNMSYNPAENAVLLCTRASNLENSTYDLYTIPKDADSQNPDAPEGKRSSGLTAVWVARNRFAVLDRMHSLLIKNLKNEITKKVQVPNCDEIFYAGTGNLLLRDADSITLFDVQQKRTLASVKISKVKYVIWSADMSHVALLAKHAIVICNRKLDALCNIHENIRVKSGAWDESGVFIYTTSNHIKYAVTTGDHGIIRTLDLPIYVTRVKGNNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLVGQSIIAYLQKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLITGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLTAATHGLDEEAESLKETFDPEKETIPDIDPNAKLLQPPAPIMPLDTNWPLLTVSKGFFEGTIASKGKGGALAADIDIDTVGTEGWGEDAELQLDEDGFVEATEGLGDDALGKGQEEGGGWDVEEDLELPPELDISPGAAGGAEDGFFVPPTKGTSPTQIWCNNSQLPVDHILAGSFETAMRLLHDQVGVIQFGPYKQLFLQTYARGRTTYQALPCLPSMYGYPNRNWKDAGLKNGVPAVGLKLNDLIQRLQLCYQLTTVGKFEEAVEKFRSILLSVPLLVVDNKQEIAEAQQLITICREYIVGLSVETERKKLPKETLEQQKRICEMAAYFTHSNLQPVHMILVLRTALNLFFKLKNFKTAATFARRLLELGPKPEVAQQTRKILSACEKNPTDAYQLNYDMHNPFDICAASYRPIYRGKPVEKCPLSGACYSPEFKGQICRVTTVTEIGKDVIGLRISPLQFR
Protein: Growth/differentiation factor 3 (GDF-3) (VG-1-related protein 2) (Q07104)
Organism: Mus musculus (Mouse)
Function: Growth factor involved in early embryonic development and adipose-tissue homeostasis. During embryogenesis controls formation of anterior visceral endoderm and mesoderm and the establishment of anterior-posterior identity through a receptor complex comprising the receptor ACVR1B and the coreceptor TDGF1/Cripto. Regulates adipose-tissue homeostasis and energy balance under nutrient overload in part by signaling through the receptor complex based on ACVR1C and TDGF1/Cripto.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9NR23}. Cytoplasm {ECO:0000250|UniProtKB:Q9NR23}. Note=Mainly accumulated in the cytoplasm. {ECO:0000250|UniProtKB:Q9NR23}.
Interaction partners:
- Activin receptor type-1C
- Activin receptor type-1B
- Activin receptor type-2B
- Activin receptor type-2A
- Teratocarcinoma-derived growth factor
- Homeobox protein NANOG
- Developmental pluripotency-associated protein 3
- POU domain, class 5, transcription factor 1
- Developmental pluripotency-associated protein 4
- Zinc finger protein 296
Sequence:
MQPYQRLLALGFLLLTLPWGQTSEFQDSDLLQFLGLEKAPSPHRFQPVPRVLRKIIRAREAAAASGASQDLCYVKELGVRGNLLQLLPDQGFFLNTQKPFQDGSCLQKVLYFNLSAIKEKAKLTMAQLTLDLGPRSYYNLRPELVVALSVVQDRGVWGRSHPKVGRLLFLRSVPGPQGQLQFNLQGALKDWSSNRLKNLDLHLEILVKEDRYSRVTVQPENPCDRLLRSLHASLLVVTLNPKHCHPSSRKRRAAISVPKGFCRNFCHRHQLFINFQDLGWHKWVIAPKGFMANYCHGECPFSMTTYLNSSNYAFMQALMHMADPKVPKAVCVPTKLSPISMLYQDSDKNVILRHYEDMVVDECGCG
Protein: EF-hand domain-containing protein (Q385C3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- SCD domain-containing protein
- Sister chromatid cohesion protein
- DNA polymerase eta
- Uncharacterized protein
- Sister chromatid cohesion protein
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- separase
Sequence:
MSLVGDVLQRVRVHAAQRRLRLNDFFTDFDKLNSGRITAGQLRRALAVNNIPVSDEEFDAITDAFAAPYTHGGSGEVTPRGAGSLVSYTNFLQALQAEEPPPELLTTLKRKPNSLSDAEEAQLRAAMQSIRDISRVRGLQLRKCFEDFDHFRSGKVSASVFRRCIPFEGLREEVIKLFIKKYKNEDGDVLYSAWCNDIEDKPQEMSQHSPTAAPLKNFLRSRSGFHTVDGLLRMLREQFSMYHLRCDDYLRDYDHFKTGFVTAPQFESALGQLRLVDAKLTAENIAMLTRAYADESTLVEKPGMDENPFVRVNYVQFLADTNPRHTEADGGSANYLAQTRAPGQFIDATNQQEQQQTEAVLRKVRQIIRSNRIHLVPTMHDFDRARKGIYEHRTCTASRFIRSLATHKIFLKPEEIELLVRRYSIRAPDGGPADEVNYFQFVMDVDEVKWDTGASRILNSSAMAELQKSVELSRPLPADTVVNVLVKIAMQAEERHLRVSEFFFDFDPLRGGTVQTDKFIVALGIAGVKLHPSEADLLKKEYASTKVRDHVDTNRFIADIGQVAPSAVPSVSTRYDFTASRSAKGEAAITLKETIQNPDDKLTAAELEELGRLRARLSHDVSSHQALLLPFFADFDRFHRAKITRTNFQQGLARHRFALTAAEIDLLSRYYAAADDKESIEYRRFVGDIGLGELAVGEFQKTINGNGATFTASLPASTCAGSTQRNVGDEEKFLDEVLLKICYFLQERKPRLAEFFPDGDELRHRHVTNSRFRHCLSILGIELTEEELRVLEISFAHPEMENHVDYPTFLAVVTHMLQNITRRMGPQQRNDSGSATTFAAYAAAGNSENLPHIAAAPPAEKATEEGDKSFHASVMDRVRRTLASRRSVSLPAFRQYDRARKGFVKEGQFFATLMSLGVQLSPAQADVLRKTYSIGGGEMGYVHFSAAVDDPRFE
Protein: Phosphatidyl-N-methylethanolamine N-methyltransferase (EC 2.1.1.71) (Phospholipid methyltransferase) (PLMT) (C8VRV0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}.
Interaction partners:
- Phosphatidylethanolamine N-methyltransferase
- diacylglycerol cholinephosphotransferase
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 2
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- MBOAT family protein, putative
- Phosphatidylserine decarboxylase family protein
- Phospholipase
- phospholipase D
- Phospholipase D1
Sequence:
MTTLSDYVDFSQDSFKYAALSIAFNPIFWNVVARAEYRSHFLTRIFGSPYRGCYFLAITIFSLGILRDHIYQQALEDQPYYAPVHQPVLGGALFAVGSVLVLSSMYALGVTGTYLGDYFGILMDAPVTGFPFNVTGSPMYWGSTLNFLGVALYKGKVAGILLTALVFVLYWFALKWEDPFTAEIYAKRERERAKSKRGGKNQ
Protein: Protein YgiW (P0ADU5)
Organism: Escherichia coli (strain K12)
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Sensor protein QseC
- Probable transcriptional regulator YgiV
- Transcriptional regulatory protein QseB
- Protein ElaB
- Uncharacterized protein YgaM
- Protein YqjC
Sequence:
MKKFAAVIAVMALCSAPVMAAEQGGFSGPSATQSQAGGFQGPNGSVTTVESAKSLRDDTWVTLRGNIVERISDDLYVFKDASGTINVDIDHKRWNGVTVTPKDTVEIQGEVDKDWNSVEIDVKQIRKVNP
Protein: Glrp1 protein (Glutamine repeat protein-1) (Q61118)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSICLFRDVAIIKSGKRRKRRAYSRLDGAKEQHQQHQQHQQDQHQQHQQQQQQQQQQQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQQQQHQQHQQHQQQQQQQQHQQHQQHQQHQHQQHQHQQHQQHQQQQQNQMDKIPGMMIFEIPETKNLERI
Protein: Floral binding protein number 7 (Q43616)
Organism: Petunia hybrida (Petunia)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRGKIEIKRIENNTNRQVTFCKRRNGLLKKAYELSVLCEAEIALIVFSTRGRVYEYSNNNIRAIIDRYKKATVETSNAFTTQELNAQFYQQESKKLRQQIQLIQNSNRHLVGEGLSSLNVRELKQLENRLERGIARIRSKKHEMILAESEDLQKREIQLEQENAFLRSKIAENERLQELSMMPAGGQEYNAIQQYLARNMLQLNMMEGVPSYPLPSDKKSLDLE
Protein: Muscle wasted, isoform C (A8DYH1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
- Multi sex combs, isoform A
- FI05704p
- Lsm10
Sequence:
MPSSAKKSDSAKSNSSTPRRPRKRKRVDRQSLDSQVDEDAKEIDRRLRKVAKKNSISAEDMQKVVRKVVRNDHVLALVTLKAEDELAREKLESAEQQKRGAIIITDTPSVPKLTRAKARELNCTPGISLPQLNETSTDNNGIEALIREDLHSDEEDEEYTFKEEDFHSDDDPNTTASDFDSNPCTPQTPLTANEESPIKFSDDGCFKVPLDRNFQDKEDLRIATRTRSKFCLQQTTIEDLQSEFVPPDVEPSDVVENEMTANDADWMQFLNDFTKPLNNTVQGDDDDPINDPEYVAADHLESEYENAEELRDVNISKKELTDLVSELFAGLLEEGVSLESIELETPQKFVESANVSMIPIDQVSRNIDFDGQQINANQQELSVFQPNLMPPPCEGNEMGMGVPVPVAVLQEETGGSACNVVNIPSEALTVPPELIAVPIPGQPNCFQIAKVVGNDSTVGLPLTEETLQNFSSLHPMEPPVVAASNGDRYKKPFDTNFTWEYISVRKHIYSEYEEKFESLRNVEPVNLNHLARSRGFTQSQHDMLQQQLRIHTQLLSQSYLQTYSHPTLYPMAKKPREMLEELHKMATKDPSFNCWNLQEAVQLVRKWEHDLSSDEFKEENEKMMDFINKETDLTDGHTRQVPRLAPRIMDLMLDSRVFMYPQYLPRMAFQPKLTQTTAYAPSEYQLIAIGLEKHLALMVKAKRQLRKGADPIRVACKRMIKDTICGKTARRIFLKIAELRNSKQYNPVKYFFEHRRAPPANAILWGFAGGLVRTPRERHMELPSGWQYYIEKTWDQKRTRRNFKASKASSVASASYLEFVREAVGEDLLLPETFGQAAVPNGSAAGSEPPKESKPKKRPAQRRPRPAENPPQLTINVNYVFGGNTSAGNIPGVSGVSVPLVAGGNLAENVLNINRSLYTAAECSSLLALPPAPPPLDENAPPAINFTVDKFTNTLQICELEESSKAVQPDLLPAQDTPSVPGRNAKRARYQIFKPKVQSANKSRKGSTPTRSRYHILRERLRHKLSQRCHSLITTYESYLRHHIEKYKDCELVQVVHNRFFALELYTQLLVDLRMFCSNTNSKTAAQPKRSRSDDEAAKLRRANRQEEMLRQMLQPDTTEERNRKDAIFAMNFYEKVEEALLSANRLDDCKKFNSILQNFDPRQEKVSSLYLKVEEILLPTHPELAEVFLNFLLPAEAAEMGKFFEHFMICNATNFINKLNIYFSKQPAQIRKIYACLNELAEMPNVSMKKVENKIMPLLKGNQFLIDWFVQQFPQGKPPKRILSPVETINLHDVQNNTTGEYTETIQEFTDVPTPSKPGCHLKYINGRIFYGAKILLPAKLSFMAASIYNEQSHDVPPVSSDSINCAHGIRAQGEKLLSMASNTDSDDGADRSEEDDASRALIIDTTSDEQNSCSSIEMCDETGLRAHAIRLNPGLYTNSSFNNAATSTPNLGNSHQSHHPHAKKTAINFGEISPRKQSAFNNSGLSPLSAAPNSSPQVDKRKSPTKKIRSPLNQTQSRQRANNQPMVVIHESQPSSSPAIECAKRLRTLIDQESVRDAADTKAGIRIIAQAKQQPPNQCSSEAITKVEVVSLDESAENMPFCTNLKMDTDQSEEELEPLQLSAGNTPQHVITTQFDSDEDCKLDVVATLANCTTTEDRSESAAALPATTSHSESGSSHSAPWTREEDKVILIEMKIGARDREQLIRRMRAKLKNRSIEELRSRHQFLMDFLSKLQGK
Protein: Internal virion protein gp7 (Ejection protein gp7) (E protein gp7) (Q01074)
Organism: Salmonella phage P22 (Bacteriophage P22)
Function: Inner capsid protein that plays a role in viral DNA ejection into the host cell. Assembles into an extracellular trans-envelope channel completed by the internal virion proteins gp7 and probably gp16. This channel allows the delivery of the viral genome into the cell cytoplasm.
Subcellular location: Virion {ECO:0000269|PubMed:328927}.
Interaction partners:
Sequence:
MLYAFTLGRKLRGEEPSYPEKGGKGGADKSAKYAAEAQKYAADLQNQQFNTIMNNLKPFTPLADKYIGSLEGLSSLEGQGQALNNYYNSQQYQDLAGQARYQNLAAAEATGGLGSTATSNQLSAIAPTLGQQWLSGQMNNYQNLANIGLGALQGQANAGQTYANNMSQISQQSAALAAANANRPSAMQSAIGGGASGAIAGAGLAKLIGSSTPWGAAIGGGIGLLGSLF
Protein: N-acetylglucosamine-1-phosphotransferase subunits alpha/beta (EC 2.7.8.17) (GlcNAc-1-phosphotransferase subunits alpha/beta) (Stealth protein GNPTAB) (UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta) [Cleaved into: N-acetylglucosamine-1-phosphotransferase subunit alpha; N-acetylglucosamine-1-phosphotransferase subunit beta] (Q3T906)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment.
Subcellular location: [N-acetylglucosamine-1-phosphotransferase subunit alpha]: Golgi apparatus membrane {ECO:0000269|PubMed:16120602, ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:25788519, ECO:0000269|PubMed:28918368}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit beta]: Golgi apparatus membrane {ECO:0000269|PubMed:16120602, ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:28918368}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- N-acetylglucosamine-1-phosphotransferase subunit gamma
- N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
- Transcriptional activator protein Pur-alpha
- Adenosine kinase
- Malate dehydrogenase, mitochondrial
- Synaptonemal complex protein 3
- DNA repair protein RAD51 homolog 1
Sequence:
MLFKLLQRQTYTCLSHRYGLYVCFLGVVVTIVSAFQFGEVVLEWSRDQYHVLFDSYRDNIAGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELQQVREQMEEEQKAMREILGKNTTEPTKKSEKQLECLLTHCIKVPMLVLDPALPANITLKDLPSLYPSFHSASDIFNVAKPKNPSTNVSVVVFDSTKDVEDAHSGLLKGNSRQTVWRGYLTTDKEVPGLVLMQDLAFLSGFPPTFKETNQLKTKLPENLSSKVKLLQLYSEASVALLKLNNPKDFQELNKQTKKNMTIDGKELTISPAYLLWDLSAISQSKQDEDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNLDNPRVTIVTHQDVFRNLSHLPTFSSPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDFYSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCSGNSGGSRYIAGGGGTGSIGVGQPWQFGGGINSVSYCNQGCANSWLADKFCDQACNVLSCGFDAGDCGQDHFHELYKVILLPNQTHYIIPKGECLPYFSFAEVAKRGVEGAYSDNPIIRHASIANKWKTIHLIMHSGMNATTIHFNLTFQNTNDEEFKMQITVEVDTREGPKLNSTAQKGYENLVSPITLLPEAEILFEDIPKEKRFPKFKRHDVNSTRRAQEEVKIPLVNISLLPKDAQLSLNTLDLQLEHGDITLKGYNLSKSALLRSFLMNSQHAKIKNQAIITDETNDSLVAPQEKQVHKSILPNSLGVSERLQRLTFPAVSVKVNGHDQGQNPPLDLETTARFRVETHTQKTIGGNVTKEKPPSLIVPLESQMTKEKKITGKEKENSRMEENAENHIGVTEVLLGRKLQHYTDSYLGFLPWEKKKYFQDLLDEEESLKTQLAYFTDSKNTGRQLKDTFADSLRYVNKILNSKFGFTSRKVPAHMPHMIDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTDQSGVLSDREIRTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYDPNLPPVTKSLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRNRFLHMHELQEWRAYRDKLKFWTHCVLATLIMFTIFSFFAEQLIALKRKIFPRRRIHKEASPNRIRV
Protein: AT16536p (Buffy) (Q8T8Y5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- BG1
- Beclin-1-like protein
- dynamin GTPase
- Apoptosome protein Dark
- Ccp84Ag
Sequence:
MPGTSYPTNNDNFSNGFPMATTQSERLLQAQNRRKFSFPATLHSASLLEVGGGPKETTRRRLSNVSDAVTRKLSYTIGWKAAQIPAQDIISQGRCLCGHYIKRRLRRSGLFNKKLGLQRIRSILGSTSMGIVRDVFPAVQVLGDELERMHPRIYNGVARQICRNPGGEFHTPDAVSLLLGAVGRELFRVEITWSKVISLFAIAGGLSVDCVRQGHPEYLPKLMESVSEVIEDELVPWINENGGWSGINTHVLPTTNSLNPLEWTTLVIGVVFGLILVFMILRFIFNLIVPKIYQRFTNS
Protein: Early E3B 14.6 kDa protein (P06498)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Down-regulates the EGF receptor and prevents cytolysis by TNF.
Subcellular location: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKFTVTFLLIICTLSAFCSPTSKPQRHISCRFTRIWNIPSCYNEKSDLSEAWLYAIISVMVFCSTILALAIYPYLDIGWKRIDAMNHPTFPAPAMLPLQQVVAGGFVPANQPRPTSPTPTEISYFNLTGGDD
Protein: Actin-2 (EC 3.6.4.-) (Actin II) (PbAct II) (Q4YU79)
Organism: Plasmodium berghei (strain Anka)
Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm. Polymerizes into longer and more stable actin filaments compared to ACT1/actin-1. Has ATPase activity. ATP hydrolysis leads to the formation of a stable intermediate ADP-inorganic phosphate (Pi) actin, which is followed by the release of Pi (Probable). ATP hydrolysis affects filament stability; ADP-bound actin depolymerizes much faster than ATP- or ADP-Pi-bound actin (Probable). Plays an essential role in male gametocyte development in the mosquito midgut, functioning in several processes including male gametocyte egress from host erythrocytes, formation of a beating flagellum and relocalization of ACT1/actin-1 to the cytoplasm. On the basal side of the mosquito midgut epithelium, required for the development of ookinetes into sporogonic oocysts.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21790945, ECO:0000269|PubMed:24471657}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8I4X0}. Note=Prior to gametocyte activation in the mosquito midgut, localizes to the cytoplasm (PubMed:21790945). Following gametocyte activation, localizes to a ring around the nucleus (PubMed:21790945). {ECO:0000269|PubMed:21790945}.
Interaction partners:
Sequence:
MPEESIALVVDNGSGMVKSGLAGDDAPKCVFPSIIGIPKMPNIMVGMEQKECYVGDEAQNKRGILTLKYPIEHGIVTNWDDMEKIWRHTFFNELRVSPEEHPVLLTEAPLNPKTNREKMTQIMFESFDVPAMYVSIQAILSLYASGRTTGIVLDSGDGVTHTVPIYEGYVLPHAINRTDMAGRDLTYYMMKLFTERGYTFTTTAEREIVRDIKEKLCYIALDYDEELKKSEERTEEVEEMYELPDGNLITVGSERFRCPEALFNPSLIGRECPGLHITAYQSIMKCDIDIRKELYNNIVLSGGTTMYNYIGERLTNEMTSLAPPSMKIKVIAPPERKYSVWIGGSILSSLSTFQKMWITKEEYDESGPSIVHRKCF
Protein: GEO07179p1 (GH11984p) (Uncharacterized protein, isoform A) (Q9VHK7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RH02303p
- Aaquetzalli, isoform A
- Hinge2
Sequence:
MRFALFAFLALCLLAFVLATPAKDTKKPATNSCQHNCGEVYEPVCAKAKNSSKERLLTFGSPCVMANYNCQHADDPFEQKSKGECGGGVSVRLS
Protein: Annexin (Q5TZZ9)
Organism: Homo sapiens (Human)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221}. Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell membrane {ECO:0000256|ARBA:ARBA00004296}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004296}; Extracellular side {ECO:0000256|ARBA:ARBA00004296}. Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cell projection, phagocytic cup {ECO:0000256|ARBA:ARBA00004231}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004284}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000256|ARBA:ARBA00004263}. Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}. Lateral cell membrane {ECO:0000256|ARBA:ARBA00004124}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
Sequence:
MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
Protein: Tumor necrosis factor alpha-induced protein 8-like protein 3 (TNF alpha-induced protein 8-like protein 3) (TNFAIP8-like protein 3) (Q5GJ75)
Organism: Homo sapiens (Human)
Function: Acts as a lipid transfer protein. Preferentially captures and shuttles two lipid second messengers, i.e., phosphatidylinositol 4,5- bisphosphate and phosphatidylinositol 3,4,5-trisphosphate and increases their levels in the plasma membrane. Additionally, may also function as a lipid-presenting protein to enhance the activity of the PI3K-AKT and MEK-ERK pathways. May act as a regulator of tumorigenesis through its activation of phospholipid signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25479791}. Cell membrane {ECO:0000250|UniProtKB:Q3TBL6}. Note=On PDGF activation, translocates from cytoplasm to plasma membrane. {ECO:0000250|UniProtKB:Q3TBL6}.
Interaction partners:
Sequence:
MGKPRQNPSTLVSTLCEAEPKGKLWVNGYAGTQGTRDATLQTRLIPLSFHLQRGKGLAAPLSALSAPRLPERPADGRVAVDAQPAARSMDSDSGEQSEGEPVTAAGPDVFSSKSLALQAQKKILSKIASKTVANMLIDDTSSEIFDELYKVTKEHTHNKKEAHKIMKDLIKVAIKIGILYRNNQFSQEELVIVEKFRKKLNQTAMTIVSFYEVEYTFDRNVLSNLLHECKDLVHELVQRHLTPRTHGRINHVFNHFADVEFLSTLYSLDGDCRPNLKRICEGINKLLDEKVL
Protein: Uridine nucleosidase 1 (EC 3.2.2.3) (Adenosine nucleosidase) (EC 3.2.2.7) (Inosine nucleosidase) (EC 3.2.2.2) (Nucleoside hydrolase 1) (Uridine ribohydrolase 1) (Xanthosine nucleosidase) (EC 3.2.2.-) (Q9SJM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in purine and pyrimidine breakdown rather than in pyrimidine salvage, especially in response to dark stress. Together with URH2, required for efficient inosine and xanthosine hydrolytic activities. Unable to use cytidine as a substrate. Can use uridine, inosine, adenosine as well as the cytokinin derivative isopentenyladenine-riboside as substrates. Hydrolyzes also xanthosine with high efficiency.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19293370}.
Interaction partners:
- Haloacid dehalogenase-like hydrolase
- Dihydropyrimidine dehydrogenase
- Uridine/cytidine kinase UKL1, chloroplastic
- Uridine kinase-like protein 4
- Uridine kinase-like protein 3
- Uridine/cytidine kinase UKL1, chloroplastic
- Uridine kinase-like protein 5
- Inorganic pyrophosphatase TTM1
- Inorganic pyrophosphatase TTM2
- Uracil phosphoribosyltransferase, chloroplastic
Sequence:
MDCGMENCNGGISNGDVLGKHEKLIIDTDPGIDDSMAILMAFQTPELEILGLTTVFGNVSTQDATRNALLLCEIAGFPDVPVAEGSSEPLKGGIPRVADFVHGKNGLGDVSLPPPSRKKSEKSAAEFLDEKVEEYPGEVTILALGPLTNLALAIKRDSSFASKVKKIVILGGAFFSLGNVNPAAEANIYGDPEAADVVFTSGADITVVGINITTQLKLSDDDLLELGNCKGKHSKLISDMCKFYRDWHVKSDGVYGVYLHDPVSFVAVVRPDLFTYKKGVVRVETQGICVGHTLMDQGLKRWNGSNPWVGYSPISVAWTVDVEGVLEYVKAKLMKP