wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear egress protein 2 (P89457)
Organism: Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.
Subcellular location: Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024}. Note=Also localizes at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
Interaction partners:
Sequence:
MAGMGKPYGGRPGDAFEGLVQRIRLIVPATLRGGGGESGPYSPSNPPSRCAFQFHGQDGSDEAFPIEYVLRLMNDWADVPCNPYLRVQNTGVSVLFQGFFNRPHGAPGGAITAEQTNVILHSTETTGLSLGDLDDVKGRLGLDARPMMASMWISCFVRMPRVQLAFRFMGPEDAVRTRRILCRAAEQALARRRRSRRSQDDYGAVVVAAAHHSSGAPGPGVAASGPPAPPGRGPARPWHQAVQLFRAPRPGPPALLLLAAGLFLGAAIWWAVGARL
Protein: Peroxisomal carnitine O-octanoyltransferase (COT) (EC 2.3.1.137) (Q9UKG9)
Organism: Homo sapiens (Human)
Function: Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl-CoA, to its corresponding carnitine ester.
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- Trifunctional enzyme subunit beta, mitochondrial
- Sterol carrier protein 2
- Peroxisomal acyl-coenzyme A oxidase 1
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Peroxisomal multifunctional enzyme type 2
Sequence:
MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQSGIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGTQLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYFRTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAALTSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIGDPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVRDIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFIQLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQQKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFVLSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAFHDMIQLMNSTHL
Protein: 3'(2'),5'-bisphosphate nucleotidase (EC 3.1.3.7) (3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase) (3'-phosphoadenosine-5'-phosphate phosphatase) (3'-phosphoadenosine-5'-phosphatase) (PAP phosphatase) (PAPase) (DPNPase) (Halotolerance protein HAL2) (Methionine-requiring protein 22) (P32179)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Involved in salt tolerance. Confers resistance to lithium.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Adenylyl-sulfate kinase
- Phosphoadenosine phosphosulfate reductase
- Sulfate adenylyltransferase
- Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase 2
- Protein APA1
- 5'-3' exoribonuclease 2
- Inositol-3-phosphate synthase
- 5'-3' exoribonuclease 1
- Probable aminopeptidase YDR415C
- Uroporphyrinogen-III C-methyltransferase
Sequence:
MALERELLVATQAVRKASLLTKRIQSEVISHKDSTTITKNDNSPVTTGDYAAQTIIINAIKSNFPDDKVVGEESSSGLSDAFVSGILNEIKANDEVYNKNYKKDDFLFTNDQFPLKSLEDVRQIIDFGNYEGGRKGRFWCLDPIDGTKGFLRGEQFAVCLALIVDGVVQLGCIGCPNLVLSSYGAQDLKGHESFGYIFRAVRGLGAFYSPSSDAESWTKIHVRHLKDTKDMITLEGVEKGHSSHDEQTAIKNKLNISKSLHLDSQAKYCLLALGLADVYLRLPIKLSYQEKIWDHAAGNVIVHEAGGIHTDAMEDVPLDFGNGRTLATKGVIASSGPRELHDLVVSTSCDVIQSRNA
Protein: Peptidoglycan-recognition protein SA (EC 3.4.17.13) (Protein semmelweis) (Q9VYX7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway upstream of spz activating enzyme SPE. Has no activity against Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SD in Gram-positive bacteria recognition. May act by forming a complex with GNBP1 that activates the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Binds to diaminopimelic acid-type tetrapeptide PGN (DAP-type PGN) and lysine-type PGN (Lys-type PGN). Has some L,D-carboxypeptidase activity for DAP-type PGN, which are specific to prokaryotes, but not for Lys-type PGN.
Subcellular location: Secreted {ECO:0000269|PubMed:11742401}. Note=Secreted in hemolymph.
Interaction partners:
- Gram-negative bacteria-binding protein 1
- Modular serine protease
- Protein immune deficiency
- Peptidoglycan-recognition protein SC1a
- Peptidoglycan-recognition protein SC2
- Gram-negative bacteria-binding protein 3
- Glycosylphosphatidylinositol anchor attachment 1
- Putative GPI-anchor transamidase
- Phosphatidylinositol glycan anchor biosynthesis class T
- Serine protease persephone
Sequence:
MQPVRFGSPWIMAIGLVLLLLAFVSAGKSRQRSPANCPTIKLKRQWGGKPSLGLHYQVRPIRYVVIHHTVTGECSGLLKCAEILQNMQAYHQNELDFNDISYNFLIGNDGIVYEGTGWGLRGAHTYGYNAIGTGIAFIGNFVDKLPSDAALQAAKDLLACGVQQGELSEDYALIAGSQVISTQSPGLTLYNEIQEWPHWLSNP
Protein: Transcription factor E2F2 (dE2F2) (E2F transcription factor 2) (E2F-like transcription factor E2F2) (O77051)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional repressor that binds to E2f sites and represses E2f-regulated target genes. Binding to E2f sites requires transcription factor Dp. Acts synergistically with Rbf2 to antagonize E2f1-mediated transcriptional activation. Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. The DREAM complex is required for recruiting E2f2 at differentiation-specific promoters and for stabilizing E2f2-Rbf complexes during S phase. During development, the complex represses transcription of developmentally controlled E2f target genes. During oogenesis, plays a role in restricting DNA synthesis to sites of chorion gene amplification in late stage ovarian follicle cells. Plays an inhibitory role in ionizing radiation (IR)-induced p53-independent apoptosis. May be involved in cell cycle exit by temporarily limiting CycE-dependent activation of E2f-regulated transcription.
Subcellular location: Nucleus {ECO:0000305|PubMed:9792788}.
Interaction partners:
- RE32990p
- Retinoblastoma family protein
- Transcription factor Dp
- LD07342p
- Protein lin-54 homolog
- Lin-52, isoform A
- Transcription factor E2f1
- LD06557p
- Myb protein
- LD05287p
Sequence:
MYKRKTASIVKRDSSAAGTTSSAMMMKVDSAETSVRSQSYESTPVSMDTSPDPPTPIKSPSNSQSQSQPGQQRSVGSLVLLTQKFVDLVKANEGSIDLKAATKILDVQKRRIYDITNVLEGIGLIDKGRHCSLVRWRGGGFNNAKDQENYDLARSRTNHLKMLEDDLDRQLEYAQRNLRYVMQDPSNRSYAYVTRDDLLDIFGDDSVFTIPNYDEEVDIKRNHYELAVSLDNGSAIDIRLVTNQGKSTTNPHDVDGFFDYHRLDTPSPSTSSHSSEDGNAPACAGNVITDEHGYSCNPGMKDEMKLLENELTAKIIFQNYLSGHSLRRFYPDDPNLENPPLLQLNPPQEDFNFALKSDEGICELFDVQCS
Protein: Malate dehydrogenase (EC 1.1.1.37) (Q8MQS7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAEPIRVVVTGAAGQIAYSLLYMIARGEVFGKDQPIVLHLLDIPPMVGVLEGVVMELADCALPLLVEVVPTTDPAVGFKDVSAAFLVGAMPRKEGMERKDLLSANVKIFRTQGQALDKFAKKDVKVLVVGNPANTNALVCSSYAPSIPRENFSAMTRLDQNRATSQIAAKLGVPISAVKNIIIWGNHSSTQYPDAGQAKVTANGTVKSVVDAINDNGYLQGSFVETVQKRGAAVIAARKMSSAMSAAKAACDHMHDWWNGTAPAQFVSMGVFSDGSYDSPKDVIFSFPVEIKNKQWKIVSGLTLSDFAKTKLSVTGKELQEEKDEALSVLDSNVSNL
Protein: Pectinesterase 4 (PE 4) (EC 3.1.1.11) (Pectin methylesterase 18) (AtPME18) (Pectin methylesterase 4) (AtPME4) (VANGUARD1-like protein 1) (VGD1-like protein 1) (O80722)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin. Plays an important role in growth of pollen tubes in female floral tissues, possibly via enhancing the interaction between the pollen tube and female floral tissues by modification of the cell walls.
Subcellular location: Secreted, cell wall {ECO:0000305}.
Interaction partners:
- Pectin lyase superfamily protein
- Probable pectate lyase 3
- Probable pectate lyase 7
- Probable pectate lyase 19
- Probable pectate lyase 5
- Probable pectate lyase 6
- Protein NRT1/ PTR FAMILY 2.8
- Cellulose synthase-like protein D1
- Pectate lyase
- Pectate lyase
Sequence:
MIGKVVVSVASILLIVGVAIGVVAFINKNGDANLSPQMKAVQGICQSTSDKASCVKTLEPVKSEDPNKLIKAFMLATKDELTKSSNFTGQTEVNMGSSISPNNKAVLDYCKRVFMYALEDLATIIEEMGEDLSQIGSKIDQLKQWLIGVYNYQTDCLDDIEEDDLRKAIGEGIANSKILTTNAIDIFHTVVSAMAKINNKVDDLKNMTGGIPTPGAPPVVDESPVADPDGPARRLLEDIDETGIPTWVSGADRKLMAKAGRGRRGGRGGGARVRTNFVVAKDGSGQFKTVQQAVDACPENNRGRCIIYIKAGLYREQVIIPKKKNNIFMFGDGARKTVISYNRSVALSRGTTTSLSATVQVESEGFMAKWMGFKNTAGPMGHQAAAIRVNGDRAVIFNCRFDGYQDTLYVNNGRQFYRNCVVSGTVDFIFGKSATVIQNTLIVVRKGSKGQYNTVTADGNELGLGMKIGIVLQNCRIVPDRKLTPERLTVATYLGRPWKKFSTTVIMSTEMGDLIRPEGWKIWDGESFHKSCRYVEYNNRGPGAFANRRVNWAKVARSAAEVNGFTAANWLGPINWIQEANVPVTIGL
Protein: Probable protease SohB (EC 3.4.21.-) (P0AG14)
Organism: Escherichia coli (strain K12)
Function: Multicopy suppressor of the HtrA (DegP) null phenotype. It is possibly a protease, not essential for bacterial viability.
Subcellular location: Cell inner membrane; Single-pass membrane protein.
Interaction partners:
- Uncharacterized oxidoreductase YciK
- Corrinoid adenosyltransferase
Sequence:
MELLSEYGLFLAKIVTVVLAIAAIAAIIVNVAQRNKRQRGELRVNNLSEQYKEMKEELAAALMDSHQQKQWHKAQKKKHKQEAKAAKAKAKLGEVATDSKPRVWVLDFKGSMDAHEVNSLREEITAVLAAFKPQDQVVLRLESPGGMVHGYGLAASQLQRLRDKNIPLTVTVDKVAASGGYMMACVADKIVSAPFAIVGSIGVVAQMPNFNRFLKSKDIDIELHTAGQYKRTLTLLGENTEEGREKFREELNETHQLFKDFVKRMRPSLDIEQVATGEHWYGQQAVEKGLVDEINTSDEVILSLMEGREVVNVRYMQRKRLIDRFTGSAAESADRLLLRWWQRGQKPLM
Protein: Probable inactive histone-lysine N-methyltransferase SUVR2 (Protein SET DOMAIN GROUP 18) (Suppressor of variegation 3-9-related protein 2) (Su(var)3-9-related protein 2) (Q9FNC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable inactive histone-lysine methyltransferase that acts as regulator of transctiptional gene silencing independently of histone H3K9 methylation. Contributes to transcriptional gene silencing at RNA-directed DNA methylation (RdDM) target loci but also at RdDM-independent target loci. Forms a complex with SUVR1 and associates with the SNF2-related chromatin-remodeling proteins CHR19, CHR27, and CHR28, thereby mediating nucleosome positioning and transcriptional silencing. Does not possess histone-lysine methyltransferase activity in vitro, and the conserved catalytic sites of SUVR2 are dispensable for its function in transcriptional gene silencing.
Subcellular location: Nucleus {ECO:0000269|PubMed:25420628}. Chromosome {ECO:0000269|PubMed:25420628}. Note=Displays two nuclear localization patterns, one forming condensed foci and the other showing diffused signals. {ECO:0000269|PubMed:25420628}.
Interaction partners:
- Helicase-like transcription factor CHR27
- Helicase-like transcription factor CHR28
- DNA-directed RNA polymerase V subunit 1
- Protein CHROMATIN REMODELING 19
- DNA-directed RNA polymerase IV subunit 1
- Protein INVOLVED IN DE NOVO 2
- Putative inactive histone-lysine N-methyltransferase family member SUVH10
- Probable inactive DNA
- Protein IDA-LIKE 2
- DNA
Sequence:
MAPNLHIKKAFMAMRAMGIEDARVKPVLKNLLALYEKNWELIAEDNYRVLADAIFDSHEDQAIQESEEKKADEVKEDEGCAAEVDRGKKKLHESIEDDEDVMAESDRPLKRLRRRGEGGSALASPSLGSPTLEGPSINDEENAPILLPYHPVPIENDHDAGELILTKVEPITNMPLSSIPDSVDRGDSSMLEIDKSNGHVEEKAGETVSTADGTTNDISPTTVARFSDHKLAATIEEPPALELASSASGEVKINLSFAPATGGSNPHLPSMEELRRAMEEKCLRSYKILDPNFSVLGFMNDICSCYLDLATNGRDSANQLPKNLPFVTTNIDALKKSAARMAYTSQASNDVVEICSNEHMRDAENGAVGDSMALVVVPECQLSADEWRLISSVGDISLGKETVEIPWVNEVNDKVPPVFHYIAQSLVYQDAAVKFSLGNIRDDQCCSSCCGDCLAPSMACRCATAFNGFAYTVDGLLQEDFLEQCISEARDPRKQMLLYCKECPLEKAKKEVILEPCKGHLKRKAIKECWSKCGCMKNCGNRVVQQGIHNKLQVFFTPNGRGWGLRTLEKLPKGAFVCELAGEILTIPELFQRISDRPTSPVILDAYWGSEDISGDDKALSLEGTHYGNISRFINHRCLDANLIEIPVHAETTDSHYYHLAFFTTREIDAMEELTWDYGVPFNQDVFPTSPFHCQCGSDFCRVRKQISKGKNVKKRA
Protein: Uncharacterized protein, isoform B (A0A0B4KGX8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPDNSNKFSASSDVRIPAWINEAYFKRLLKREFREFRRILNLSIIPATPPGETYTSLLMRIVIDIELKDGFSQQKSYIVKTMLDDAQGNGGFVNTLNIFPKEKMMYETIIPNLEQLYEEAGLSVKFAPKCHHAEDIKGRICLVQEDLQTKKYRNINRLKGFDMAHMHRVLEKLAEFHAAGAVWRQRKGPFPDDFQRIYLPANYQKSKSYQARLQSYKTAIASWGLADHEQYVSRIPTADQFVQSYASCFNNNPQEFKVLNHGDFWSSNIMLSYTQTGDINQVRFVDFQLCKWGSPAQDLWELIICSARHSIRIQYFDYFIRIYHTHLVRCLKILKYSERIPMLRELHMSMIKYGFWGYFTTFTHLVFILLPPDTEASLVKLTQPGEEGDRFRSKVYTNPLYVRSALSIFPFLLRRGILDF
Protein: Large ribosomal subunit protein mL46 (39S ribosomal protein L46, mitochondrial) (Q9W086)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL16m
- Mitochondrial ribosomal protein S11
- Small ribosomal subunit protein uS15m
- Mitochondrial ribosomal protein L2
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein mL44
Sequence:
MLRRIVQVGARELSRAQSSTASAEKWDLYAGVLVERLPVVSKSLNPLEKQFQDLLWRVEYENSLKSDHELKHEREIVQAELIKQGKIQVDLEDAGSKQTAQDLKDAYVEELKKFQLGSRTTPDDQANRTTSTDRCLDDTLYLLVQQKLGQQEHLILPQGKREEGESMRQTAERVLRESCGQELQVLFYGNAPVGFHKYKYPRNQRTETVGAKVFFYRASLRSGQVPENLTKFEWLPKEALNEKLTNTAYAQSVKKFLL
Protein: GEO07854p1 (RE53289p) (Troponin C 25D) (Troponin C at 25D, isoform A) (Troponin C at 25D, isoform C) (Q9VMT2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Myosin light chain alkali
- Myosin regulatory light chain 2
- Tropomyosin-2
- Troponin T, skeletal muscle
- RE24163p
- Troponin I
- GH21596p
- Myosin heavy chain, muscle
Sequence:
MEDDEKMDIMRKAFQMFDTQKTGFIETLRLKTILNSMGQMFDDSELQALIDDNDPEDTGKVNFDGFCSIAAHFLEEEDAEAIQKELKEAFRLYDREGNGYITTSTLKEILAALDDKLSSSDLDGIIAEIDTDGSGTVDFDEFMEMMAGE
Protein: Pyoverdine synthetase D (Q9I182)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PvdJ
- PvdL
- MbtH-like domain-containing protein
- Pyoverdine biosynthesis protein PvdE
- L-ornithine N
- Probable non-ribosomal peptide synthetase
- phosphoribosylglycinamide formyltransferase 1
- Pyochelin synthetase PchE
- Probable non-ribosomal peptide synthetase
- PvdG
Sequence:
MQALIEKVGSLSPQERKALAVLLKQQGVNLFEIAPVFKRQDGEPLRLSYAQERQWFLWQLEPESAAYHIPSVLRLRGRLDLDALQRSFDSLVARHETLRTRFRLDGDEARQEIAASMALPLDIVALGPLEEGALARQVETTIARPFDLERGPLLRVSLLRLAEDDHVLVLVQHHIVSDGWSMQVMVEELVQLYAAYSRGLEVALPALPIQYADYALWQRSWMEAGEKERQLAYWTGLLGGEQPVLELPFDRPRPVRQSHRGAQFILELDIDLSQALRRVAQQEGATAFALLLASFQALLYRYSGQADIRVGVPIANRNRVETERLIGFFVNTQVLKADLDGRMGFDELLAQARQRALEAQAHQDLPFEQLVEALQPERSLSHNPLFQVLFNYQSEARGNGQAFRFDELQMESVQFDSRTAQFDLTLDLTDEEQRFCAVFDYATDLFDASTVERLAGHWRNLLRGIVANPRQRLGELPLLDAPERRQTLSEWNPAQRECAVQGTLQQRFEEQARQRPQAVALILDEQRLSYGELNARANRLAHCLIARGVGADVPVGLALERSLDMLVGLLAILKAGGAYLPLDPAAPEERLAHILDDSGVRLLLTQGHLLERLPRQAGVEVLAIDGLVLDGYAESDPLPTLSADNLAYVIYTSGSTGKPKGTLLTHRNALRLFSATEAWFGFDERDVWTLFHSYAFDFSVWEIFGALLYGGCLVIVPQWVSRSPEDFYRLLCREGVTVLNQTPSAFKQLMAVACSADMATQQPALRYVIFGGEALDLQSLRPWFQRFGDRQPQLVNMYGITETTVHVTYRPVSEADLEGGLVSPIGGTIPDLSWYILDRDLNPVPRGAVGELYIGRAGLARGYLRRPGLSATRFVPNPFPGGAGERLYRTGDLARFQADGNIEYIGRIDHQVKVRGFRIELGEIEAALAGLAGVRDAVVLAHDGVGGTQLVGYVVADSAEDAERLRESLRESLKRHLPDYMVPAHLMLLERMPLTVNGKLDRQALPQPDASLSQQAYRAPGSELEQRIAAIWSEILGVERVGLDDNFFELGGHSLLATRVISRVRQEQQLDASLKALFERPVLEAFAQGLERTTDAVSTIPLADRQQPLALSFAQERQWFLWQLEPESAAYHIPSALRLRGRLDVDALQRSFDSLVARHETLRTRFRLEGGRSYQQVQPAVSVSIEREQFGEEGLIERIQAIVVQPFDLERGPLLRVNLLQLAEDDHVLVLVQHHIVSDGWSMQVMVEELVQLYAAYSQGLDVVLPALPIQYADYALWQRSWMEAGEKERQLAYWTGLLGGEQPVLELPFDRPRPARQSHRGAQLGFELSRELVEAVRALAQREGASSFMLLLASFQALLYRYSGQADIRVGVPIANRNRVETERLIGFFVNTQVLKADLDGRMGFDELLAQARQRALEAQAHQDLPFEQLVEALQPERNASHNPLFQVLFNHQSEIRSVTPEVQLEDLRLEGLAWDGQTAQFDLTLDIQEDENGIWASFDYATDLFDASTVERLAGHWRNLLRGIVANPRQRLGELPLLDAPERRQTLSEWNPAQRECAVQGTLQQRFEEQARQRPQAVALILDEQRLSYGELNARANRLAHCLIARGVGADVPVGLALERSLDMLVGLLAILKAGGAYLPLDPAAPEERLAHILDDSGVRLLLTQGHLLERLPRQAGVEVLAIDGLVLDGYAESDPLPTLSADNLAYVIYTSGSTGKPKGTLLTHRNALRLFSATEAWFGFDERDVWTLFHSYAFDFSVWEIFGALLYGGRLVIVPQWVSRSPEDFYRLLCREGVTVLNQTPSAFKQLMAVACSADMATQQPALRYVIFGGEALDLQSLRPWFQRFGDRQPQLVNMYGITETTVHVTYRPVSEADLKGGLVSPIGGTIPDLSWYILDRDLNPVPRGAVGELYIGRAGLARGYLRRPGLSATRFVPNPFPGGAGERLYRTGDLARFQADGNIEYIGRIDHQVKVRGFRIELGEIEAALAGLAGVRDAVVLAHDGVGGTQLVGYVVADSAEDAERLRESLRESLKRHLPDYMVPAHLMLLERMPLTVNGKLDRQALPQPDASLSQQAYRAPGSELEQRIAAIWAEILGVERVGLDDNFFELGGHSLLLLMLKERIGDTCQATLSISQLMTHASVAEQAACIEGQARESLLVPLNGRREGSPLFMFHPSFGSVHCYKTLAMALRDRHPVKGVVCRALLGAGREVPEWDDMVAEYAEQLLQEHPEGVFNLAGWSLGGNLAMDVAARLEQRGRQVAFVGWIDAPAPVRVEAFWNEIGPTPEAVPNLSVGEMRVELLGVMFPERAEHIERAWSSICSATTDDEQRWTRMSDWAEAEIGAEFATLRSEIAQSNELEVSWELKQILDERLKAMDYPRLTAKVSLWWAARSTNAIQRSAVERSMAEAIGAERVEPVRVLDTRHDKIIDHPEFVQSFRAALERAGR
Protein: Caveolin-1 (Vesicular integral-membrane protein VIP21) (P33724)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000269|PubMed:10816572, ECO:0000269|PubMed:8385608}; Peripheral membrane protein {ECO:0000250}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:8385608}. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae. {ECO:0000250|UniProtKB:P49817, ECO:0000250|UniProtKB:Q03135}.
Interaction partners:
- Caveolin-2
- Tyrosine-protein kinase.
- Integrin beta
- Receptor protein-tyrosine kinase.
- Caveolin
- Dynamin 2
- Major prion protein
- Calmodulin like 4.
- Calmodulin like 5.
- Integrin beta
Sequence:
MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMAEEMSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPFFEAVGKIFSNIRINMQKET
Protein: Shadow of prion protein (Protein shadoo) (Q5BIV9)
Organism: Homo sapiens (Human)
Function: Prion-like protein that has PrP(C)-like neuroprotective activity. May act as a modulator for the biological actions of normal and abnormal PrP (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Mitochondrial ribosome-associated GTPase 1
- Prion-like protein doppel
- Major prion protein
- GTP-binding protein 4
Sequence:
MNWAPATCWALLLAAAFLCDSGAAKGGRGGARGSARGGVRGGARGASRVRVRPAQRYGAPGSSLRVAAAGAAAGAAAGAAAGLAAGSGWRRAAGPGERGLEDEEDGVPGGNGTGPGIYSYRAWTSGAGPTRGPRLCLVLGGALGALGLLRP
Protein: Sulfotransferase (EC 2.8.2.-) (F1RD72)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Alpha-tocopherol transfer protein
- Retinal pigment epithelium-derived rhodopsin homolog
Sequence:
MDLPDISSIKSPSRPEIFEFAGIPMISYFTKNWEKLKNFQARPDDILIATYPKAGTTWVSYILDLLYFGKVDPNGQSSLPIYMRVPFLESCFPGMPSGTELADNLPNSPRLIKTHLPVQLVPKSFWEQNSRVVYVARNAKDNVVSYFHSDRMNHGQPEPGDWNTFLEDFLKGEVVFGSWFDHVCGWWEKKKTYPNLHYMLYEDMAKDINGEVESLCTFLKLSRSDEEKNKIINSVQFDAMKQNKMTNYSTIPTMDFKISPFMRKGKVGDWKNHFTLAQNEQFDEVYKQKMKNTTLNFRTKI
Protein: Type II secretion system protein M (T2SS protein M) (Cholera toxin secretion protein EpsM) (General secretion pathway protein M) (P41851)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in the complex assembly and recruits EpsL resulting in a stable complex in the inner membrane. Provides thus a link between the energy-providing EpsE protein in the cytoplasm and the rest of the T2SS machinery.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Type II secretion system protein L
- Type II secretion system protein N
- Type II secretion system protein J
- Type II secretion system protein K
- Type II secretion system protein H
- Type II secretion system protein C
- Type II secretion system protein I
- Type II secretion system ATPase E
- Type II secretion system core protein G
- Type II secretion system protein F
Sequence:
MKELLAPVQAWWRSVTPREQKMVMGMGALTVLAIAYWGIWQPLSERTAQAQARLQTEKQLLSWVSENANDIVTLRAQGGSDAPSDQPLNQVITNSTRQFNIELIRVQPRGEMMQVWIQPLPFSQLVSWIAYLQERQGVSVDAIDIDRGKVNGVVEVKRLQLKRGG
Protein: Ribonuclease VapC32 (RNase VapC32) (EC 3.1.-.-) (Toxin VapC32) (P9WF73)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB32.
Interaction partners:
- Antitoxin VapB32
- Ribonuclease VapC29
- Ribonuclease VapC25
- Ribonuclease VapC33
- Ribonuclease VapC28
- Ribonuclease VapC11
- Ribonuclease VapC26
- Ribonuclease VapC39
- Ribonuclease VapC4
- Ribonuclease VapC15
Sequence:
MILVDTSVWIEHLRAADARLVELLGDDEAGCHPLVIEELALGSIKQRDVVLDLLANLYQFPVVTHDEVLRLVGRRRLWGRGLGAVDANLLGSVALVGGARLWTRDKRLKAACAESGVALAEEVS
Protein: E3 ubiquitin-protein ligase ATL6 (EC 2.3.2.27) (RING-H2 finger protein ATL6) (RING-type E3 ubiquitin transferase ATL6) (Q8RXX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro. May be involved in the plant C/N response and the early steps of the plant defense signaling pathway.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- F3H9.15 protein
- Transmembrane protein
- Uncharacterized membrane protein At3g27390
- DUF4228 domain protein
- U-box domain-containing protein 14
- At1g29190/F28N24_12
- Uncharacterized protein At1g76660
- Uncharacterized protein At5g17350
Sequence:
MRSSDHMAFAGVLPIVFLLILSSADLAASQSQPGPTNQPYNYGRLSPAMAVIVVILIAALFFMGFFSIYFRHCSGVPDAGVSPAGGARSRATVNAAARGLDVSVVETFPTFLYSDVKTQKLGKGELECAICLNEFEDDETLRLLPKCDHVFHPHCIDAWLEAHVTCPVCRANLAEQVAEGESVEPGGTEPDLELQQVVVNPEPVVTAPVPEQLVTSEVDSRRLPGVPVDLKRVKFSRSHTTGHSVVQPGECTERFTLRLPEDVRKRIMKDWKLNRTNSLLVLPRGGSSRRGKPIDRSRARSDRWLFRKTPSFLWRSRDDGSIRLGATGSVRASAVPNSTGSDSVRAGDRWAFLRNASFLWRNSSVHVPRGGVNKDGEGTSVKSTGASGSTSGSVRLPV
Protein: Matrix metallopeptidase 28 (epilysin) (Q5SSG2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVAGVSLLLRALPLLLWGCQDAQPTQHGLPELRQEAEAFLEKYGYLSEQGSKAPASAQFRNAIREFQWISQLPLSGVLDQATLRQMTRPRCGVADTDSHATWTERISTLLAGHRAKMRRKKRFAKPGNKWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLANAFDGPGGALAHAFLPRRGEAHFDGDERWSLSRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDALLSWDDVLAVQSLYGKPLGRSVATQLPGKVFTDFEAWDPHNSQSRRPETRGPKYCHSSFDAITVDGQWRLYVFKGSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGTGRRKDREQTPFPSGNY